PEROXI DASES

1970 - 1 - 9 ~ O
PEROXIDASES
1970 1980
A SURVEY OF THEIR BIOCHEMICAL AND
PHYSIOLOGICAL ROLES IN HIGHER
PLANTS
Thomas GASPAR, Claude PENEL, Trevor THORPE
:"......
and Hubert GREPPIN
UNIVERSIT DE GENVE - CENTRE DE BOTANIQUE
GENVE 1982
Thomas GASPAR
Head Laboratory of Fundamental and Applied Hormonology, Botanical
Institute, University of Lige, Belgium, and Lecturer, University of
Genve, Switzeriand.
Claude PENEL
Chef de Service, Laboratory of Plant Physiology, and Lecturer, University
of Genve, Switzeriand.
Trevor THORPE
Professor of Botany, Department of Biology, University of Calgary,
Canada. Past-Chairman of the International Association for Plant Tissue
Culture.
Hubert GREPPIN
Professor of Plant Physiology and Ecophysiology, Head Laboratory of
Plant Physiology, Past-Chairman Department of Biology Department,
Dean Faculty of Sciences, University of Genve, Swtzeriand.
1
ACKNOWLEDGEMENTS
It is a pleasure to acknowledge the support of the Centre de Botanique
and the Centre Universitaire d'Informatique of Genve, which made
this volume possible. The authors express their appreciation to their
respective secretary-typists for their cooperation, and particularly to
Mrs. Christiane Tschopp for her assistance with the editorial work on
the word processing machine BG-lOOO. Thomas Gaspar and Claude
Penel thank the University of Genve as weil as the Swiss and Belgian
National Science Foundations which facilitated the scientific exchanges
between Genve and Lige.
CONTENTS
PART ONE
Chapter 1. INTRODUCTION 3
Chapter 2. CHEMISTRY AND BIOCHEMISTRY
OF PEROXIDASES 9
2.1. CHEMICAL STRUCTURE 9
2.\.\. Prosthetic group 10
2.1.2. Protein \1
2.1.3. Compounds 13
2.2. FORMATION OF COMPOUNDS l, II and III
AND CATALYTIC REACTIONS 14
2.2.\.
2.2.2.
Reaction mechanisms in presence of H
2
0
2
Reaction mechanisms in absence of H
2
0
2
17
19
2.3. PARTICULAR PEROXIDASE REACTIONS 21
2.3.1. Types of reactions and substrates 21
2.3.2. IAA degradation 25
2.3.3.
2.3.4.
H
2
0
2
formation and .Iignin biosynthesis
Ethylene biosynthesis
33
44
2.4. TYPES OF PEROXIDASES 48
1
Chapter 3. ISOPEROXIDASES:
FACT OR FICTION ? 61
Chapter 4. SUBCELLULAR LOCALIZATION AND
BIOSYNTHESIS OF PEROXIDASES 71
4.1. CELLULAR LOCALIZATION OF PEROXIDASES 71
4.1.1. TechnicaI aspects 71
4.1.2. Cellular localization 73
4.2. BIOSYNTHESIS OF PEROXIDASES AND
ITS REGULATION 79
4.2.1. De nova synthesis or activation 79
4.2.2. Transcription 80
4.2.3. Translation 81
4.2.4. Post-translational steps and secretion 82
Chapter 5. PHYSIOLOGICAL PROCESSES
MEDIATED BY PEROXIDASES 89
5.1. AUXIN CATABOLISM 90
5.1.1. Growth 91
5.1.2. Morpho- and organogenetic processes 97
5.2. LIGNIN FORMATION 101
5.2.1. Growth 101
5.2.2. Ditferentiation, vascularization 102
5.3. DEFENSE MECHANISMS AGAINST
PATHOGENS 103
5.4. RESPIRATION 107
5.5. UGHT MEDIATED PROCESSES 108
5.5.1. Peroxidases as pigments 108
5.5.2. Peroxidases and phytochrome 109
5.5.3. Photoperiodic control and flowering 112
!
,-:
Chapter 6. PRACTICAL APPLICATIONS
OF PEROXIDASES 123
Chapter 7. CONCLUDING REMARKS
AND PROSPECTS 131
PART TWO
REFERENCES 137
AUTHOR INDEX 255
ORGANISMIC INDEX 303
SUBJECT INDEX 313
. j
i
ccc
ABBREVIATIONS
ACC
C l, Il, III
CCP
con A
2,4-0
DAB
DCP
DHF
EDTA
EGTA
Fe J+
P
Fe 2+
P
GA
GC-ECO
GLC-ECD
1-aminocycJopropane- 1-carboxylic acid
Compound l, Il, III
2-chloro-ethyltrimethylammonium chloride
cytochrome c peroxidase
concanavalin A
2,4-dichlorophenoxyacetic acid
3,3'-diaminobenzidine
2,4-dichlorophenol
dihydroxyfumarate
ethylenediamine tetraacetic acid
ethylene glycol-bis (2-aminoethylether)
N,N'-tetraacetic acid
ferriperoxidase
ferroperoxidase
gibberellic acid
gas chromatography - electron capture detection
gas liquid chromatography - electron capture detection
HRP
IAA
Kapp
KMBA
NAD
SAM
horseradish peroxidase
indole-3-acetic acid
apparent dissociation constant
cx-keto-y-methylthiopropionaldehyde
nicotinamide adenine dinucleotide
S-adenosyl-methionine
3 N O ~ H V d
CHAPTER 1
INTRODUCTION
Peroxidases (donor : H
2
0
2
oxidoreductase; EC. 1.11.1. 7) are
enzymes, whose primary function is to oxidize molecules at the expense
of hydrogen peroxide. Since they are widely distributed in living
organisms, and show dramatic color-product formation as a resultof
their catalytic effect, these enzymes have been among the most extensively
investigated since the beginnings of enzymology (1459).
Perhaps the earliest report on peroxidase activity was in 1855 by
Schonbein, who observed that certain organic compounds could be
oxidized by dilute solutions of hydrogen peroxide in the presence of
substances occurring in plants and animais (Saunders et al., 1964).
The name peroxidase was first given by Linossier, who in 1898 isolated
it from pus.
Studies carried out in the period up to 1918 showed that peroxidase
activity was widely found in plants. Relatively pure peroxidase was
also obtained during this period. It was also shown that the peroxidase
system could oxidize pyrogallol, gallic acid and certain amines (Saunders
et al., 1964).
During the period 1918-1931, the enzyme was purified, and the
determination of its activity was carried out by assessing the oxidation
of pyrogallol to purpurogallin. In 1931 it was shown that peroxidase
was a hematin (Saunders et al., 1964). The last 50 years has seen an
exponential increase in the number of people working on peroxidase,
so much so that during the 1970-1980 period sorne 1600 plus references
have appeared on the enzyme (see bibliography Section).
The phenomenon of peroxidase multiplicity has been known for
many years but it was not until the development of the zymogram
technique by Hunter and Market (1957) that the occurence of
isoperoxidases came under extensive investigation. It is now an established
4 PEROXIDASES 1970/1980
fact that most enzymes exist in multiple molecular forms. Tt is further
acknowledged that a large amount of the variation detected in isozyme
studies has a genetic base, thus rendering isozymes as useful markers
in the analysis of gene functions and metabolic regulation in growing
and differentiating cells and tissues (1159).
Peroxidase is probably the enzyme appearing under the largest
number of isoforms (up to 42 in horseradish, ref. 584) in plants
examined.. This fact makes them suspect as native molecules as such
(see Chapter 3) and automatically renders studies involving isoperoxidases
doubtful as to their real significance. The problem is further complicated
by the obligatory or non-obligatory enzyme intermediate Compounds
l, II and III and the relative specificity towards a wide range of hydrogen
donors such as phenolic substances, cytochrome c, nitrite, leuco-dyes,
ascorbic acid, indole amines, and certain inorganic ions, especially the
iodide ion. Moreover, besides peroxidasic oxidation of electron donor
molecules, various reactions have been found to be catalyzed by
peroxidase. These are aerobic oxidations of dihydroxyfumarate (Swedin
and Theorell, 1940; Chance, 1952), IAA (see Section 2.3.2), triose
reductone (Yamazaki et al., 1956), NADH (Akazawa and Conn, 1958;
Yokota and Yamazaki, 1965) and naphthohydroquinone (Klapper and
Hackett, 1963), hydroxylation of aromatic molecules (Mason et al.,
1957; Buhler and Mason, 1961), formation of ethylene (see Section
2.3.4), halogenation (Morrison et al., 1970; Hager et al., 1970) and
antimicrobial activity (see Section 5.3).
If the cornmon feature of these reactions appears to be an
involvement of HzO
z
' from the point of view of function, however,
peroxidase is rather similar to oxidase, the name of which is now used
in a narrow sense for electron transfer oxidases. The name 'oxygenase'
is restricted to enzymes that catalyze the incorporation of atmospheric
oxygen into substrate molecules (Hayaishi, 1974). Thus based on the
acceptor specificity and by analysis of final reaction products, the
distinction between electron transfer oxidase, oxygenase and peroxidase
appear to be weil established (1459).
Reaction of mixed types suchas monooxygenase (mixed function
oxidase by Mason's (1957, 1965) terminology) and peroxidase-oxidase
have been reported. If peroxide is an intermediate product of Oz
reduction it might be said that in many cases peroxide metabolism is
involved as a part of the overall oxygen metabolism. Detailed analysis
of the mechanism of Oz metabolism have revealed that three types of
reactions are correlated in complicated ways as indicated below :
5 INTRODUCTION
oxidase (electron transfer)
I ~
oxygenase .. ~ peroxidase
The recently established idea of the oxyferroperoxidase structure for
so-called Compound III would make it easy to relate the function of
peroxidase- with those of electron transfer oxidase and oxygenase (1459,
see Chapter 2).
Peroxidases have the capacity to catalyze a large number of
biochemical reactions. In plants and in animais, they apparently fulfil
many different functions and certainly we are far from knowing
everything about them. Their ubiquity and their biochemical versatility
explain why peroxidases are the subject of so many publications. But
despite the fact that peroxidases are among the most studied enzymes,
or, perhaps due to the great number and the diversity of the articles
devoted to their study, there has been no comprehensive review, since
Saunders, Holmes-Siedle and Stark published their book in 1964. That
book essentially dealt with the biochemical aspects of peroxidases.
Since that time, peroxidases have been extensively examined in biological
and physiological studies.
One major objective of the present book is to gather in one place
the references of articles concerned with peroxidases that have appeared
during the last ten years. These references coyer ail the aspects of
peroxidase research (biochemistry, physiology, genetics, histo- and
cytochemistry). This bibliographic matter mainly concerns higher plant
peroxidases, but there are also a few hundred references dealing with
animal or human biology. These latter are of general interest. Three
indexes (authors names, subjects and organisms) facilitate the search
of references. The second major objective is to critically review what
is known about the enzyme. Thus, the reader will also find several
chapters covering all aspects of the peroxidase story.
It is our hope that this book, which is written by plant physiologists
from a physiological viewpoint, will be of value to all people working
with peroxidases. For those unfamiliar with the enzyme we hope that
our synthesis of the available information will lead to a clearer
understanding of peroxidase, the most extensively examined enzyme
in plants.
6
PEROXIDASES 1970/1980
REFERENCES
For numbered references in the text, see bibliographical section
AKAZA\VA, T.; CONN, E.E. 1958. The oxidation of reduced
pyridine nucleotides by peroxidase. J. BIOL. CHEM. 232: 403
415.
BUHLER, D.R.; MASON, H.S. 1961. Hydroxylation catalyzed by
peroxidase. ARCH. BIOCHEM. BIOPHYS. 92: 424-437.
CHANCE, B. 1952. Oxidase and peroxidase reactions in the presence
of dihydroxymaleic acid. J. BIOL. CHEM. 197: 577-589.
HAGER, L.P.; THOMAS, J.A.; MORRIS, D.R. 1970. Studies on
the relationship ofchloroperoxidase - halide and chloroperoxidase
hydrogen peroxide complexes to the mechanism of the halogenation
reaction. In 'BIOCHEMISTRY OF THE PHAGOCYTIC
PROCESS'. Schultz, J. (Ed.). North-Holland Publ., Amsterdam,
pp. 67-87.
HAYAISHI, O. 1974. General properties and biological functions
of oxygenases. In 'MOLECULAR MECHANISMS OF OXYGEN
ACTIVATION'. Hayaishi, O. (Ed.). Academie Press, New York,
pp. 1-28.
HUNTER, R.L.; MARKERT, C.L. 1957. Histochemical
demonstration of enzymes separated by zone electrophoresis in
starch gels. SCIENCE 125: 1294-1295.
KLAPPER, M.H.; HACKETT, D.P. 1963. The oxidatic activity of
horseradish peroxidase. II. Participation of ferroperoxidase.
J. BIOL. CHEM. 238: 3743-3749.
MASON, H.S. 1957. Mechanisms of oxygen metabolism. ADV.
ENZYMOL. 19: 79-233.
MASON, H.S. 1965. Oxidases. ANN. REV. BIOCHEM. 34: 595-634.
MASON, H.S.; ONOPRYENKO, 1.; BUHLER, D.R. 1957.
Hydroxylation: The activation of oxygen by peroxidase.
BIOCHIM. BIOPHYS. ACTA 24: 225-226.
MORRISON, M.; BA YSE, G.; DANNER, D.J. 1970. The role of
mammalian peroxidase in iodination reactions. In
'BIOCHEMISTRY OF THE PHAGOCYTIC PROCESS'. Schultz,
J. (Ed.). North-Holland Publ., Amsterdam, pp. 51-66.
INTRODUCTION 7
SAUNDERS, Re.; HOLMES-SIEDLE, A.G.; STARK, RP. 1964.
Peroxidase. The properties and uses of a versatile enzyme and
sorne related catalysts. Butterworths, London, 271 p.
SWEDIN, B.; THEORELL, H. 1940. Dioximaleic acid oxidase action
of peroxidases. NATURE 145: 71-72.
y AMAZAKI, 1.; FUJINAGA, K.; TAKEHARA, 1.; TAKAHASHI,
H. 1956. Aerobic oxidation of triose reductone by crystalline
tumip peroxidase. J. BIOCHEM. 43: 377-386. '
YOKOTA, K.; YAMAZAKI, 1. 1965. The activity of the horseradish :
peroxidase compound Ill. BIOCHEM. BIOPHYS. RES. COMM.
18: 38-53.
CHAPTER 2
CHEMISTRY AND
BIOCHEMISTRY OF PEROXIDASES
Today, much is known about the chemistry and biochemistry of
peroxidases. As a matter of fact, much more has been definitively
determined in this area than on any other aspect of the peroxidase
story. In this chapter, we will discuss the chemical structure, the
formation of various peroxidase compounds and their catalytic
mechanisms, specifie peroxidase reactions and final1y the ditferent types
of peroxidases known to date.
2.1. CHEMICAL STRUCTURE
Peroxidases and isoperoxidases have been purified from ditferent
plant material and it appears that they do not significantly ditfer in
size (from 40,000 to 50,000 daltons), absorption spectrum and activity
(Theorell, 1942; Jermyn and Thomas, 1954; Paul, 1958; Klapper and
Hackett, 1965). They are formed (Fig. 1a) from a colourless glycoprotein
combined to a brown-red ferriporphyrin (Fig. 1b).
10
PEROXIDASES 19701 J 980
o
Peroxidase
1
1 1
Protohaematin IX: Glycoprotein
L
r 1
Fe
3
+
Protoporphyrin :IX
,r
CH
2
CH
C H ~ C H 2
H
3
C
H3
C CH3
CH2
/
CH2
\.
/ C ~
HO "'0
Protohaematin JX
Fig. J. a. Structure of peroxidase.
b. Structure of protohaematin IX.
2.1.1. Prosthetic group
The prosthetic groups of horseradish peroxidase (HRP), Japanese
radish peroxidase, cytochrome c peroxidase (CCP) and chloroperoxidase
are known to be ferriprotoporphyrin IX (Fig. lb). Its spectrum gives
the same general picture, with bands ex, 13 and y, as that of other
metallic phorphyrins (Nari and Penon, 1968; 432). The heme groups
in animal peroxidases are much more tightly bound to the protein
that are the hemes in plant peroxidases (1459).
CH
2
"CH
2
/
C
cf 'OH
BIOCHEMISTRy Il
2.1.2. Protein
Little was known about the chemical structure of peroxidases until
relatively recently. Amino acid analysis have been carried out for
isoenzyme preparations of HRP (Shannon et a/., 1966; 1208), for two
isoenzyme preparations of Japanese radish peroxidase (Morita and
Kameda, 1959; Shimizu and Morita, 1966), two peroxidases of wheat
(619), five peroxidases from turnip and horseradish (1425) and eight
isoperoxidases of tobacco (680). About 300 residues of 16 amino acids
were found together with +/- 20% sugars (glucose, galactose, mannose,
arabinose, xylose, fucose, hexosamine).
The first complete amino acid sequence of a plant peroxidase was
obtained by Welinder (1424). A refined analysis of the quantitatively
dominant HRP peroxidase C among the isoperoxidases of horseradish
root (l424a) indicates that it consists of a hemin prosthetic group,
2Ca
2
+ and 308 amino acid residues, including 4 disulfide bridges, in
a single polypeptide chain that carries 8 neutral carbohydrate side
chains. The molecular weight of the polypeptide chain is 33,890.
Assuming an average carbohydrate composition of (Gle NAc)2' Man
3
,
Fuc, Xyl for each carbohydrate chain, the molecular weight of native
HRP C is close to 44,000. The complete amino acid sequence of
turnip peroxidase P
7
has since also been determined and compared to
that of HRP C (853, 854).
The calcium binding by two HRP isoenzymes has been confirmed
and already has been related to its properties (530, 966). Calcium
particularly contributes to maintaining the structural conformation of
the protein as indicated by the effects of calcium removal (by guanidine
hydrochloride and EDTA) on the thermal stability of the protein.
Calcium-free HRP isoenzyme C, but not isoenzyme A, can be
reconstituted upon addition of calcium and regains enzymatic activity.
Free calcium readily exchanges with isoenzyme C, but only to a small
extent with isoenzyme A (530). ft must be mentioned that sorne
isoperoxidases apparently do not contain carbohydrate (679, 1054).
ft appears on the other hand that sorne soluble (Shannon et al.,
1966; 904) and cell wall bound (283) peroxidases might contain
hydroxyproline.
12 PEROXIDASES 1970/1980
The conformation of different HRP and tumip isoenzymes has
been investigated by means of circular dichroism, and it has been
suggested that although the active sites are similar, sorne small differences
did exist (Strickland et al., 1968; 624), and that the isoenzymes differed
in amino acid and carbohydrate compositions (Mazza et al., 1968;
851). Since their secondary structures appeared to be very similar, it
was suggested that only a few amino acid residues around the heme
group goVem the spectral characteristics. It was shown that peroxidases
from tumip and an isoperoxidase from horseradish contain highly
homologous peptides, thought to be located in proximal and distal
positions of the heme iron (1425).
The environment surrounding the heme of CCP has been found
to be hydrophobie (Asakura and Yonetani, 1969). This is possibly the
case with ail plant peroxidases. The hydrophobie structure of the heme
environment of myoglobin and hemoglobin was disclosed by X-ray
analyses.
The influence of the heme environment on physicochemical
properties and catalytic activity is clearly manifested in the peroxidase
isoenzymes from tumip. Thus the most basic isoperoxidase P differs
7
from the other tumip enzymes in possessing low peroxidase and high
'oxidase' activities towards IAA (627, 852). The electronic structure
of the heme and the tertiary structure of the heme crevice are essentially
the same in the acidic tumip peroxidases, PI and Pz, and isoperoxidase
P
7
(1438). The postulated difference between PI and P
7
, i.e., that a
carboxyl group is replaced by a histidine residue as distal groups of
the proteins, is in agreement with the amino-acid content of the proteins
(1102).
A possibility that the fifth coordination position in HRP is occupied
by an imidazole group of the protein was suggested by several workers
(Brill and Williams, 1961; Nakamura et al., 1963; 1208, 1474a). By
elaborate experiments using '4NO, Yonetani (1474a) concluded that
the fifth ligand of the heme iron in CCP and HRP may be the imidazole
group of a histidine residue and that the unpaired electron of NO sits
in the sixth coordination position although it is considerably delocalized
to the heme iron and the proximal nitrogen in these NO compounds
of ferrous peroxidases.
13 BJOCHEMISTRY
2.1.3. Compounds
Peroxidase reacts with numerous substances (cyanide, fluoride, etc.)
and fonus with them stable complexes which can be detected by
spectrophotometry. The enzyme can also be reduced by strong reductants
such as. hydrosulfite, methylviologen semiquinone, etc. : the
ferroperoxidase fonu is then generated. It shows a low affinity towards
cyanide (Keilin and Hartree, 1955) but a high specificity in binding
carbon monoxide to fonu the photodissociable carboxyferroperoxidase.
Cyanide and CO then were often used during peroxidase catalyzed
reactions in order to detect the ferri- and/or the ferroperoxidase forms.
Ferroperoxidase also reacts with oxygen to form oxyferroperoxidase.
~
1
E
~ '\:J
~ u 100
1
~
-
1
1
ID
1
1
1
UJ
E
~
1
l
TT
-
T
E
U
T
5 ~
-
E
W
400
500 600 700
wovelenglh (nm)
Fig 2. Absorption spectra offerriperoxidase (P) and Compounds 1, II and III (from 432).
Plant peroxidases generally fonu with peroxides three types of
compounds called Compounds J, II and III, which have characteristic
absorption spectra (Fig. 2). The state of the knowledge of the electronic
structure of the heme in these three compounds has been given by
Yamazaki (1459) and further studied by several authors (106, 225a,
625, 628, 633, 678, 1002, 1004).
14 PEROXIDASES 1970/1980
2.2. FORMATION OF COMPOUNDS l, Il AND III
AND CATALYTIC REACTIONS
Peroxidase Compounds 1 and II are formed in the presence of
low peroxide concentration only. The green Compound l appears first.
It is further transformed in Compound II through reduction by an
electron donor. The following reactions have been confirmed for the
peroxidase catalysis of its characteristic one-electron oxidation of donor
molecules :
Peroxidase + HzO
z
- - - - + ~ Compound l
Compound 1 + AH
2
~ Compound II + AH"
Compound II + AH ~ peroxidase + AH"
z
2AH- ~ A + AH (or AH - AH)
z
Compounds 1 and Il are thus considered to be obligatory enzyme
intermediates in an overall peroxidase reaction regenerating the original
ferriperoxidase.
Judged by the hyperfine structure of the electron spin resonance
spectra, the free radicals derived from several donor molecules in the
above reactions were judged to be free in solution (Yamazaki et al.,
1960; Piette et al., 1961). These free radicals are very reactive, and
their reactions will result in a variety of peroxidase functions (see below).
Compound III has been identified as a product formed in the
presence of excess HzO
z
(Keilin and Hartree, 1951; George, 1953). It
was shown by Chance (1952) and George (1953) that Compound III
was formed from the reaction of Compound Il and H
Z
02" On the other
hand, Yokota and Yamazaki (1965) observed that Compound III
disappeared in the presence of electron donors and acceptors to give
ferriperoxidase, which led them to propose the fol1owing reactions :
15 BIOCHEMISTRY
+e
Compound III
------........ Fe
p
3+ + H
2

2
(Fe 2+0 ) (2H+)
P 2
or
-e
Compound III -------+. Fe
p
3+ +
2
(Fe 3+0-)
p 2
This makes Compound III a hybrid between the complexes
ferroperoxidase-oxygen and ferriperoxidase-superoxide anion.
This also would mean that Compound III can react with
ferroperoxidase and Compound II (Bjorksten, 1968; 1033) :
C III + ferroperoxidase --+ 2 ferriperoxidase + H
2
0
2
CIII+CII ----+ 2 ferriperoxidase + 02
An oxyferroperoxidase structure has been suggested for peroxidase
Compound III (Mason, 1957, 1958; George, 1952; Yamazaki & Piette,
1963; Yamazaki el al., 1965). This idea, however, was not generally
accepted since reduced peroxidase was thought to be oxidized to the
ferric enzyme without an intermediate similar to Compound III (Theorell,
1947; Harbury, 1957). Recently, the oxyferroperoxidase structure of
Compound III has been confirmed on the basis of the following data :
(a) Ferroperoxidase reacted with oxygen to form Compound III, when
excess hydrosulfite that reduced Compound III was not present
(Yamazaki and Yokota, 1965; Yamazaki el al., 1966; Wittenberg
el a/., 1967).
(b) Compound III was formed by photolysis of an aerobic solution of
CO-ferroperoxidase (Blumberg et a/., 1968; 1312).
(c) Titrimetric experiments showed that Compound III was at a three
equivalent oxidized state above the ferric enzyme (Wittenberg et
a/. , 1967; 1312; Yamazaki el a/., 1968).
16 PEROX]DASES 1970/1980
Fig. 3. The live redox states of HRP. The numbers in the circles indicate the
effective oxidation number of heme. See Yamazaki (1459) for the oxidation
potentials.
Figure 3 shows the relationship between the five redox forms of
HRP. Ali these forms can be obtained in fairly stable states under
suitable experimental conditions and have been crystallized using a
basic HRP preparation, named 'isoenzyme F'. Higher oxidation forms
of HRP can be reduced to the ferric enzyme by various electron
donars. The most active form is Compound 1. ]t has been shown that
nitrous acid (Chance, 1952) and p-aminobenzoic acid (Chance and
Ferguson, 1954) reduce Compound ] 100 and 25 times faster than
Compound Il. Similar results have been obtained by Cormier and
Prichard (1968) with luminol, by Dunford and colleagues with
ferrocyanide (532) and iodide (1120, 1122), and by Yamazaki et al.
(1 460a) with ascorbic acid and anthranilic acid. The conversion of
HRP Compound] to the ferric enzyme without an appreciable formation
of Compound II was reported by Bjorksten (117) and Roman and
Dunford (1120), using iodide as an electron donor.
HRP Compound III also reacted with various electron donars
which are not autoxidizable (Yamazaki et al., 1965; 1312; Yokota
and Yamazaki, 1965). Compound III was less reactive with electron
donars than Compound Il, while in the absence of such donars
Compound II was less stable than Compound III. The stability of
Compound Il varied greatly with enzyme preparations, but that of
Compound III was almost independent of the purity of the enzyme
preparations (13 J 2).
17 BIOCHEMISTRy
HRP Compound III was shown to undergo spontaneous decay to
the ferric enzyme without detectable intermediates like Compounds 1
and II (Yamazaki el al., 1966; Wittenberg el al., 1312). This might
be explained by assuming that the oxidative decomposition of Compound
III occurs in the presence of one-eJectron oxidants such as Compounds
1 and II.
Compound III + e- , peroxidase + Oz
Rate constants of the reactions of Compound III with Compounds 1
and II can be measured. However, the release of Oz during the reaction
has not been confirmed. For the decomposition of Compound III a
mechanism, in which dissociation of Compound III into Compound
II and HzO
z
is rate limiting, was proposed (1312), but this needs further
proof.
The reaction of Compound III with electron donors is of particular
interest. Undoubtedly, Oz is activated when it combines with
ferroperoxidase. It might be reasonable to assume that Compound III
is reduced by electron donors via the intermediates Compound 1 and
II. As mentioned above, these intermediates are much more active
oxidants for the electron donors used so far. Therefore, an ingenious
device would be needed to identify the intermediates in the reduction
process of Compound III.
The direct conversion from ferrous HRP to Compound II was
demonstrated by Noble and Gibson (950).
2.2.1. Reaction mechanisms in presence of HO
z z
During the course of peroxidase reactions, oxygen is consumed.
This a priori couId be due to two quite different processes :
- a direct interaction of the reduced hemoprotein formed during
the reaction with oxygen,
18 PEROXIDASES 1970/1980
- a reaction with oxygen of intermediary unstable degradation
products of the electron donor.
ln the former case, the formation of Compound III during the reactions
has to be considered. In the latter one, only Compounds 1 and II
would play a role.
The formation of Compound III during the aerobic oxidation of
dihydroxyfumarate (DHF) (Swedin and Theorell, 1940; Lemberg and
Legge, 1949; Mason, 1958; Yamazaki and Piette, 1963; Yamazaki et
al., 1965) and NADH (Yokota and Yamazaki, 1965) catalyzed by the
system peroxidase-H
2
0
2
has been observed. This formation as well as
that of ferroperoxidase might be the result of secondary reactions and
Compound III would not be necessarily involved in the 'peroxidation'
pathway mediated essentially by Compounds 1 and II.
The transitions C 1 to C II and C II to Fe 3+, coupled with
electron donor oxidations, give rise to donor radicals (yamazaki et al.,
1960; Ray, 1962; Parups, 1969). The reaction of these reducing radicals
with oxygen certainly permits the use of the gas during the peroxidase
reactions. This reaction subsequently generates a superoxide radical
which itself would oxidize another donor molecule and thereby would
contribute to the propagation of a free radicals' chain as illustrated in
Figure 4.
-----_ .... ------ ,
: 1
1
1
1
1
1
1
1
1
1
1
,
1
1
1
1
CN
1
1
1
1
1
AH"'" "'0
2
1
1
l ' , 1
L ~
Fig. 4. Oxidation mechanism of an e1ectron donor (AHz) by the peroxidase-peroxide
system. The enclosed part corresponds to the free radicals's chain propagation
(afier Yamazaki, 1958 and Ricard and Nari, 1967).
BIOCHEMISTRY 19
In this mechanism, there would be no reaction of the enzyme
with oxygen at any time and the formation of Compound III, as
already mentioned above, would be the result of a reaction between
Fe 3+ and the superoxide radical.
p
2.2.2. Reaction mechanisms in absence of H 0
2 2
Substances such as hydro- and naphthoquinones (Klapper and
Hackett, 1963) and IAA (see 432) can be oxidized by peroxidase in
the absence of peroxide being introduced in the reaction mixture. The
medium has been suspected of containing peroxide traces from the
beginning and more peroxide could be formed later on through
autooxidation of electron donors.
Klapper and Hackett (1963) however did not exclude the possibility
of a direct reduction of ferriperoxidase into ferroperoxidase by the
electron donors and therefore proposed a mechanism of peroxidase
oxidation without participation of peroxide (Fig. 5). An analogous
mechanism involving ferriperoxidase reduction and the subsequent
formation of the reactive oxyferroperoxidase (C III) has been proposed
by Ricard and Nari (1966) for IAA oxidation (see below).
c:r"
2
7' '>. COMPOUND /II
(FepOJ+)
AH AH2
A+
Hp
2 A+H 0
2
COMPOUND 1/
(Fe
p
0
2
+)
Fil? 5. Oxidation mechanism of hydro- and naphthoquinones (alier Klapper and
Hackett. (963).
20 PEROXIDASES 1970/1980
The peroxidase mediated IAA oxidation in the absence of peroxide
has also been explained by Fox et al. (1965, 1968) through an interaction
of ferriperoxidase with oxygen and IAA in order to form a compound
identical to C 1. This C 1 would further generate C II which would
oxidize IAA. The following sequence has been proposed :
Fe 3+ + 0 ------+. Fe 3+0
p 2 p 2
Fe 3+0 + IAA -----+. CI
p 2
e
CI -----.... CIl
C II + IAA -----....... Fe 3+ + IAA"
p
This IAA- radical would finally react with oxygen as does the AH in
the Yamazaki's scheme (Fig. 4).
The binding of different hydrogen donars and inhibitors to peroxidase
will not be examined here, although it has been studied by several
authors (744,1162).
21 BIOCHEMISTRy
2.3. PARTICULAR PEROXIDASE REACTIONS
2.3.1. Types of reactions and substrates
Substrate Product Reference
Oxidation with H 0
2 2
acetosyringone dimethoxyquinone 1476
2,2' -azino-di- corresponding 217
(3-ethyl-benzthia- azodication
zoline-6-sulphonic
acid) (ABTS)
benzidine benzidine blue Maehly and Chance
(1954)
betacyanin unknown 723
chlorophyllides unknown 840
chlorpromazine semi-quinone free radical 239
crocin unknown 325
N,N-dialkyl- secondary amines + 421a, 422
anilines aldehydes
o-dianisidine bis (3,3' -dimethoxy- Moller and
4-amino)azo-biphenyl Ottolenghi
(1966)
22
dihydroxyphenyl
alanine
di-isopropyl-N
nitrosamine
ferulic acid
guaiacol
3-hydroxy
flavone
indolyl-3
acetaldehyde
kaempferol
leuco-malachite
green
lignins
pyridoxal
pyrogallol
scopoletin
vanillic acid
PEROXIDASES 1970/1980
dopachrome
hydroxy-N-nitrosamine
unknown
tetraguaiaco1
salicylic acid +
phenylglyoxylic acid +
benzoic acid
indole-3-carbaldehyde
2,3,4,5,7,4'-penthydroxy
flavanone + p-hydroxy
benzoic acid
malachite green
corresponding qui nones
unknown
purpurogallin
unknown
dehydrovanillic acid
84
349
1036
Maehly and Chance
(1954)
1178
1467
573
Maehly and Chance
(1954)
1476
566
Maehly and Chance
(1954)
1085
97
23
Oxidation with Oz
dihydroxymaleie
aeid (Mn
z
+)
dithiothreitol
NAD(P)H(Mn
z
+,
ROH)
2,4,6/3,5 penta
hydroxyeyclohexane
(Mn
z
+)
phenylaeetal
dehyde (Mn
z
+)
phenylpyruvate
(Mn
z
+, DCP)
2',4,4'-trihydroxy
ehalcone
4,2',4'-trihy
droxy-ehalcone
BIOCHEMISTRy
diketomaleie aeid +
HzO
z
disulfide bond
NAD(P)
DL-3,5/4,6-tetra
hydroxyeyclohexane
1,2-dione
benzaldehyde +
forroie aeid
unknown
3,4',7-trihydroxy
flavanone + 4',6
dihydroxy-2-(a.
hydroxybenzyl)
eoumaranone
benzoxepinone-spiro
eyclohexadienone
4',7-dihydroxyflavon-3-o1
Chance (1952)
973
Akazawa and
Conn (1958)
681a
350
618
1076
1149
996
24
Decarboxylation
oxaloacetate (Mn
2
+)
syringic acid
vanillic acid
Halogenation
tyrosine + r
(or 1)
2
Hydroxylations
p-hydroxyphenyl
acetonitrile (Mn
2
+)
tyrosine
tyrosine (DHF)
PEROXIDASES 1970/1980
malonate Shannon, de VeiHis
and Lew (1963)
2,6-dimethoxy-p 97,703
benzoquinone
4,4'-dimethoxy-2,5, 97
2'5'-dibenzoquinone
methoxy-p-benzoquinone 703
3-monoiodotyrosine 85
p-hydroxymandelonitrile 765
dihydroxyphenylalanine 997
dihydroxyphenylalanine Buhler and Mason
(1961)
Polymerization (condensation)
phenol 0,0' -biphenol 273
tyrosine dimer (0,0' -biphenyl
linkage)
lignins
83
25 BIOCHEMISTRY
2.3.2. IAA degradation
Evidence has accumulated which indicates that the reaction of
HRP with IAA differs from those with other substrates such as NADH
and DHF. It is indeed very interesting to note here a feature of IAA
HRP reactions that is rather similar to an oxygenase type. Through
the efforts of many workers (Kenten, 1955; Ray, 1956; Ray and
Thimann, 1956; Morita et al., 1962; 1967; Hinman and Lang, 1965)
the following stoichiometry has been confirmed :

.. ) + 2
N
H lperoxidase

or

+C02 +H2
0
H
The products were found to be indole-3-aldehyde and 3-methylene
oxindole. Morita et al. (1962) showed that the dominant product was
indole-3-aldehyde when higher enzyme concentrations were used.
Apparently the reaction is similar to the lactate oxidative decarboxylase
reaction, which is monooxygenase type (Bloch and Hayaishi, 1966) or
an internai mixed function oxidase type (Mason, 1965). Indole-3-acetic
acid was found to react with HRP Compound III at a relatively high
rate (Yamazaki et al., 1965; Yokota and Yamazaki, 1965; 1312). In
this respect the reaction is similar 10 the tryptophan pyrrolase reaction,
in which the oxygenated enzyme was considered to be an obligatory
intermediate (Ishimura et al., 1967; 605a). Many features of the
mechanism of the IAA reaction, however, still remain to be elucidated.
The key points of the mechanism can be summarized as follows :
26 PEROXIDASES 1970/1980
a. The IAA free radical formed by peroxidase catalysis is an important
intermediate (Hinman and Lang, 1965; Morita et al., 1967; Yamazaki
and Souzu, 1960; Ray, 1960, 1962; Ricard and Nari, 1966, 1967;
924). Hinman and Lang (1965) proposed a mechanism in which
the radical reacts with molecular oxygen to fonn 3-methylene
oxindole as a main product through several nonenzymic steps (Fig.
6a). Although it is unknown whether the radical is free or attached
to the enzyme, it may react with external oxidants such as ferric
cytochrome c and ferric o-phenanthroline complexes (Yamazaki
and Souzu, 1960). A question which arises is why the nature of
the final products depends upon the concentration of enzymes in
the reaction (Morita et al., 1962, 1967; Hinman and Lang, 1965).
An answer to this question is proposed through the reaction scheme
(Fig. 6b) of Bemiller and Colilla (90). The proposed pathway requires
as a key step a two-electron oxidation catalyzed by a metal ion,
be it the iron of the peroxidase heme or Mn
3
+. It is proposed that
the enzyme oxidizes Mn
2
+ to Mn
3
+ and that IAA is subsequently
oxidized non-enzymatically by Mn
3
+ to 3-methylene-indolenine with
the kind and amount of subsequent products being detennined by
the pH and composition of the reaction mixture. This scheme also
explains the ability of cx-methyl-IAA and cx,cx-dimethyl-IAA to act
as substrates for peroxidases, while indole-3-propionic and indole
3-butyric acids cannat.
b. During the reaction with IAA a part of the enzyme, spectrally
similar ta Compounds II and III is observed as an intennediate
(Morita et al., 1967; Yamazaki and Souzu, 1960; Ricard and Nari,
1966, 1967; Fox et al., 1965; Degn, 1969; 697, 875). From the
visible spectrum between 500 and 600 nm the intennediate is judged
to be Compound III at around pH 4.0 (Morita et al., 1967) and
Compound II at pH 5.0 (Fox et al., 1965; 1461). It has been
concluded that Compound III, accumulated during the reactions of
DHF and NADH, is not a Michaelis type of intennediate (Chance,
1952; Yokota and Yamazaki, 1965; Yamazaki and Piette, 1963).
Since IAA .!eacts
!2te, .
must have a positIve maniQKin the catalysis. However, it is still
uncertam proceeds via Compound
II or III, mainly because of the difficulty in distinguishing between
these two HRP compounds.
"(06) 1l1l!10.) pUll J;JII!W;J8 J;J!JV "q
"(Zn7 oS11l ;J;Js) 961 'l}ul11 pUll UIlWU!H J;J!JV "11
UO!lllpI1Jl};Jp VV( JOj SlillM41lld p;JsodoJd
c
- ~ - ~
:I:% I% 9
o
%8.
~ 4 o
0-0-0
8
40
8
l 1 N
o n
n/ ni
IO
<9 ~
@ J'

N
n
l
8
o
o
- ~ l
I%
N ~
8
l
A1I1.SIW3H:J0I8
28 PEROXIDASES 1970/1980
c. A small amount of HzO
z
eliminates the lag phase and promotes
the 0z-consuming oxidation of IAA under certain experimental
conditions (Kenten, 1955; Yamazaki and Souzu, 1960; Ray, 1960,
1962; Shin and Nakamura, 1962; Morita et al., 1967). It is also
true that the inhibition by catalase is negligible under certain
experimental conditions (Fox et al., 1965; 1461). Consequently, the
raie of HzO
z
does not appear to be essential even as an initiator
of the reaction. Using superoxide dismutase, it has recently been
found that superoxide anions are not involved in the reactions of
IAA with HRP (875, 1461). This fact seems to be a peculiar
property of the IAA reaction since the oxidations of NADH and
DHF by HRP are strongly inhibited by superoxide dismutase (1461).
This fact is compatible with the mechanism (Hinman and Lang,
1965; Ray, 1962) that the IAA peroxide radical instead of the
superoxide anion radical is a product of the reaction between the
IAA radical and Oz (see also 697). A significant question to be
answered is how the IAA radical can be formed without an
involvement of the superoxide anions. An answer to this question
is given by Ricard and Nari. The mechanism they praposed (852;
Nari, 1967; Nari et al., 1967; Ricard and Nari, 1966; Ricard and
Nari, 1967; Ricard, 1969) involves the effective participation of
ferroperoxidase in IAA oxidation (already postulated by Ray, 1960),
at acidic pH and is based on the following arguments :
1) Carboxyferroperoxidase is partially decomposed by light (Iight
suppresses the CO inhibition of IAA-oxidase) not into ferro- but
into ferriperoxidase. CO inhibition and its suppression by light
argue against the participation of a unique free radicals'chain.
Thus contrary to Yamazaki's opinion, peroxidase reduction
cannot be entirely due to highly reducing radicals generated
through prior formation of Compounds 1 and II. Furthermore
peroxidase reduction is obtained in a medium in such poor
oxygen content that IAA destruction does not occur and evidently
in these conditions, IAA autooxidation cannot occur and
consequently no peroxide can be formed.
2) Substances such as IBA (indolebutyric acid), IPA (indolepropionic
acid) which appear unable to reduce peroxide (and indicators
such as methylene blue, Laught violet and phenosafranin which
are reduced by IAA) are not degradable in the absence of peroxide.
29 BIOCHEMISTRy
3) The impossibility of a complete inhibition of IAA degradation
by high catalase concentrations (Iargely sufficient to completely
inhibit the typical peroxidation of IBA and IPA) which cannot
be interpreted otherwise than by a partial IAA oxidation without
a peroxide requirement.
4) Cyanide does not stop the reaction when added during its course.
When present in the mixture before the reaction initiation, the
reaction is completely blocked even in presence of H 0
2 2
Ricard's group furthermore demonstrated that Compound III
(obtained by reduction of ferriperoxidase in the presence of
methylviologen and 0) is decomposed by IAA which is simultaneously
destroyed. This was confirmed by Yamazaki et al. (1967). Indoleacrylic
acid is similarly destroyed by Compound III (429).
Klapper and Hackett's proposaIs and partiail y those of Yamazaki's
group were integrated in a summary scheme (Fig. 7a) by Ricard and
Nari (1966).
This scheme shows that IAA can be destroyed in the absence of
peroxide :
a) either through a typical peroxidase reaction (peroxide is formed in
the mixture) involving Fe 3+, C l, C II and free radicals of IAA,
p
b) or through a cycle involving Fe 2+ and C III.
p
The latter functions only at acidic pHs (3 to 4), is blocked by
carbon monoxide (to form carboxyferroperoxidase) and by ferricyanide
(which oxidizes Fe 2+ into Fe 3+) as weil. The former peroxidase reaction
is insensitive to these two The whole system is dependent
upon the IAA-mediated ferriperoxidase reduction into ferroperoxidase.
Employing stopped-flow and low-temperature spectroscopic
techniques, Ricard and Job (110 1) further elucidated the reaction
sequences and the nature of the intermediate peroxidase compounds
leading either to indole-3-aldehyde or to methyleneoxindole (Fig. 7b).
30 PEROXIDASES 1970/1980
COMPfUNO Il
o
COMPOUND 1
[:0.
----.f

3
+
IAA f

ox
---- COMPOUND 1I1..Jl--IAA

r
P2 !_
IAA peroxide.LIA- FeJ+ IAA
3-methyleneoxindole j
;s:
: 2+
COMPOUND 1 !'d Fep ----.,
IAA
;:::::::,. epoxIe +
lAI>: COMPOUNUDI COMPOUND III
1AAi Jt
Fe
3
+IAA Fe
3
+0'
IAA-? 2 p r
Oz
3+ F':+3+0.-
Fe 2+
I
AAO-
Fep IAA0
2
CO
2
ep 2 IAA
P 2
l:AA
21 A A' 4 \ FeJ+epoxide
indole-3-aldehyde
u
O
2
CO
2
1AA' ---":::::""'IAAOi ..{>3-methyleneoxindole
Fig. 7. a. Possible pathways for IAA degradation by HRP(afier Ricard and Nan, 1966).
b. 1. Proposed reaction sequences for the oxygen consuming degradation
of IAA.
II. Non-enzymatic evolution of IAA free radical to methylene oxindole
(afier Ricard and lob, 110 1).
BIOCHEMISTRY 31
It can be added that the ferric enzyme could be reduced by the
IAA free radical rather than by IAA itself (924). In addition to these
pathways, it must be mentioned that a considerable amount ofperoxidase
is inactivated during the oxidation of IAA (Fox et al., 1965). The
process of heme degradation has been described by Yamazaki (1459).
Isoenzymes involved in IAA destruction
To date, three hypotheses, with varying degrees of substantiating
evidence, have been suggested in relation to the molecular 'residence'
(582) of IAA oxidase activity. The first considers that the two types
of activity (i.e., IAA oxidase and peroxidase) are present on separable
and distinct enzymes; the second considers that the two types of activity
are resident on one enzyme (peroxidase) but with two active centers;
and the third calls attention to the presence of peroxidase isoenzymes
where one member of the family of isoenzymes may be the primary
residence of IAA activity. These alternatives are examined briefly.
The idea of separate enzymes was reported by Sequeira and Mineo
(1966). They had noted that fresh preparations (tobacco roots) lost
IAA oxidase activity after several weeks in storage, whereas peroxidase
activity was unchanged. Further, they found that thermal inactivation
points and pH optima were different. Attempts to separate the two
types of activity on columns of silica gel, carboxymethyl cellulose,
diethylaminoethyl cellulose, and diethylaminonethyl Sephadex failed,
but with SE-Sephadex and 0.1 M eluting buffer they reported a major
IAA oxidase peak (at 5.4 elution volumes) with little or no peroxidase
activity from both tobacco root extracts and commercial HRP. Hoyle
results (582) obtained with the same HRP and a purified Betula enzyme
preparation did not support Sequeira and Mineo's contention.
The belief that both types of activity reside in one enzyme (i.e.,
peroxidase) is more widely held. Evidence offered in support of this
belief is mainly that both types of enzyme activity remain together
through various stages of purification and also there is evidence that
thermal inactivation is the same for both (Ray, 1960). The work of
Siegel and Galston (1967, confirmed by Hoyle, 582) suggests that the
dual catalytic functions of peroxidase may result from two active sites
on the enzyme. By separating the apoenzyme from its heme prosthetic
group with acidified acetone, they found that apoenzyme alone would
32 PEROXIDASES 1970/1980
oxidize IAA, but was devoid of peroxidase activity. However, partial
restoration of peroxidase activity occurred with recombination of heme
and apoenzyme. They concluded that apoenzyme possesses the IAA
oxidase function, and that a heme-protein attachment is needed for
the peroxidase function.
Their work was challenged by Ku et al. (709) who used a mixture
of an acid and butanone (instead of the acid-acetone) for dissociation
of the heme group from its apoenzyme and were not able to effect
the oxidation of IAA in the presence of the apoenzyme alone or with
Mn
2
+ and DCP as cofactors. The residual enzyme activity of the
apoenzyme thus might be due to a slight contamination by unresolved
holoenzyme in that fraction rather than to the apoenzyme itself.
In most studies, the total oxidase and/or peroxidase activity has
been measured without consideration of the multiple forros of an
enzyme (i.e. isoenzymes). MacNicol (1966) has separated four isoenzymes
(three cationic and one neutral) from Alaska peas. He found that aIl
of the isoenzymes could catalyze the peroxidation of guaiacol and the
oxidation of IAA, but the C cationic species had an IAA oxidase
J
guaiacol peroxidase ratio that was 10-fold higher than the next most
acti ve species.
There is probably no example in the literature of a peroxidase
extract or purified isoperoxidase unable to develop a so-called IAA
oxidase activity in vitro when placed in suitable conditions of pH and
effectors, and/or after adequate purification (473). The question thus
is whether any peroxidase isoenzyme encounters such favourable
conditions - and IAA - in situ in order to develop the auxinolytic activity.
IAA destruction capacity of different types of isoperoxidases has
been studied in vitro (697, 852, 1101). Mazza et al. (852) and Ricard
et al. (1102) established a strong positive correlation between the
oxygenase IAA-destroying activity (in absence of exogenously supplied
peroxide or other cofactors) of different purified turnip peroxidases and
their midpoint oxido-reduction potential value. They concluded that
the most basic isoenzyme was the best candidate to be 'IAA-oxidase'
in vivo. Nakajima and Yamazaki (924) showed that the oxygen-consuming
oxidation of IAA occurred much faster in the presence of the HRP
neutral isoenzyme C than in the presence of the acidic isoenzyme A.
Physiological studies, which attempt to establish a relationship between
endogenous IAA level, intensity of the IAA-dependent process and
prior qualitative changes in peroxidase zymograms generally support
the view that auxin catabolism is mediated by the most cationic
isozymes (see Section 5.1).
BIOCHEMISTRy 33
The oxidation of IAA by a purified anionic tomato peroxidase
(697) was found to be negligible unless reaction mixtures were
supplemented with H
2
0
2
A similar dependence on H
2
0
2
has been
shown for the IAA oxidase-peroxidase complex of yellow birch (587).
From a physiological standpoint, such a result suggests that the
destruction of IAA in tissue could be controlled by the availability of
H
2
0
2
or other peroxides, as probably are lignin and ethylene biosynthesis.
This view was first expressed by Siegel and Galston (1955) and has
been extended to coyer the role of auxin protectors (1281).
2.3.3. H 0 formation and lignin biosynthesis
2 2
Metabolic pathways leading to the main families of plant phenolic
compounds are relatively weil known. Shikimic acid and cinnamic
acid pathways constitute a common sequence from which originate
the different groups of polyphenols and lignin particularly (Fig. 8).
The pathway of lignin biosynthesis and the enzymes involved are
weil established. Several excellent recent reviews treat these subjects
in detail (20,890a). Phenylalanine ammonia Iyase (PAL) catalyzes the
conversion of phenylalanine to trans-cinnamic acid. Cinnamic acid is
hydroxylated at the para position by cinnamic acid-4-hydroxylase to
form p-coumaric acid; however, p-coumaric may also be formed by
the deamination of tyrosine catalyzed by tyrosine ammonia Iyase. p
Coumaric acid is further hydroxylated by p-coumaric acid hydroxylase
to give caffeic acid. o-Methyltransferase then methylates caffeic acid
to ferulic acid. Sinapic acid is formed by hydroxylation and methylation
of ferulic acid. Coumaric, ferulic, and sinapic acid are converted to
their respective CoA esters by cinnamate acid-CoA-ligase. The esters
of cinnamic acid derivatives are reduced to the corresponding aldehydes
and further reduced to alcohols by cinnamoyl-CoA-oxidoreductase and
cinnamyl alcohol dehydrogenase. These enzymes would form the
cinnamylic alcohols into the secretory vesicles during their migration
towards the wall.
34 PEROXIDASES 1970/1980
phenylalanine

cinnamic acid caffeic acid

ft
%,OPiC
acid
CoA esters
tyrosine
cinnamyl aldehydes
cr
lignins
4@1---
cinnamyl alcohols
Fig. 8. Metabolic pathway and enzymes involved in lignin biosynthesis:
l. phenylalanine ammonia Iyase 2. cinnamic acid-4-hydroxylase
3. p-coumaric hydroxylase 4. o-methyltransferase 5. cinnamic acid-CoA
ligase 6. cinnamoyl-CoA-oxidoreductase 7. cinnamyl alcohol
dehydrogenase 8. peroxidases.
Polymerization due to peroxidase could begin during this transport
(20). Polycondensation of the cinnamyl alcohols probably occurs through
the mediation of wall peroxidases. Free radicals, formed by oxidation
of these alcohols by peroxidase-H
2
0
2
exist in several resonance forms
and couple in an essentially random manner, although participation
of the more stable resonance forms is statistically favored. Coupling
between radicals of the alcohols occurs readily. In the lignifying plant
cell wall, however, coupling is primarily between incoming radical
species and the growing lignin polymer which itself contains phenolic
hydroxyl groups that are oxidized to radicals by peroxidase.
BIOCHEMISTRY 35
Since different esters of cinnamic acids have been identified in
sorne lignins, it is conceivable that sorne vesicles, unfused and lacking
reductases, directly bring their esters to the wall, where further trans
esterification occurs.
A review of the available data on the localization in the cell of
the enzymes of phenolic metabolisrn, the organization of the different
sequences at the subcellular level, the existence of transport processes
between different organelles and finally the participation of soluble and
wall-peroxidases in lignin formation and integration in the wall has
been presented schematically (Fig. 9) by Alibert et al. (20),
pheny 1- alanine
----------t------------------
ENDOPL ASMIC
RETICULUM --------i-----i-------------j---
GOLGI cinnamic
A PPARATUS caffeic acids
'd
p - cou
!.
ma ri c .der
P
0 x 1 ose s
. . oc 1 s
SECRETORY
VESICLES
Slna!1C
p-coumarate-CoA
sinapate-CoA
cinntmYliC alcohols
dimerization .. _
poly mer iz a tian
ci nnom y 1icii 9 ni ilS '1i-- - - - - - - - - - - - - - Pe r 0 x id ose s
esters -----___.
WALL
bound to li gn ins - - - - - - -H
2
0
2
Fig 9. Fonnation of lignin precursors and lignin in the cell (after Alibert el al.. 20),
36 PEROXIDASES 197011980
Peroxidase involvement
On the basis of histochemical studies, Freudenberg et al. (1952)
proposed that peroxidase was involved in lignification in vivo in spruce.
This view was supported by the work of Jensen (1955), and Siegel
(1956, 1957) who later demonstrated that peroxidase would efTect an
in vitro oxidation of eugenol to a lignin-like substance. Later studies
by Van Fleet (1959), Wardrop and Bland (1959), and Koblitz and
Koblitz (1966) argued against the direct involvement of peroxidase in
the lignification process. In particular these workers have shown that
maximum peroxidase activity occurs in prolignifying tissues, and that
activity declines after lignification of the primary wall has commenced.
Further, De Jong (1967) daims never to have observed a positive
peroxidase reaction in xylem.
The discrepancies might come from the fact that sorne observations
concemed ail the year xylem without distinguishing the difTerentiating
stages. A more recent study by Czaninski (264) indeed showed that
during the difTerentiation of wheat vascular cells, longitudinal primary
walls exhibit a strong peroxidase activity. A similar reaction can be
visualized in transverse walls but in this case, the contrast decreases
sharply at the beginning of secondary wall deposition.
It is evident from studies such as those of Lipetz and Garro (1965)
and Parish and Miller (1969), that there may be sorne relationship,
even though an indirect one, between peroxidase and lignification.
These workers have shown that treatments which cause leaching of
wall-bound peroxidases also reduce lignification.
Isolated cell wal1s from Pinus ellioUii tissue cultures produce lignin
having physical and chemical properties similar to that prepared from
wood, when incubated in the presence of coniferyl alcohol and HzO
z
.
The enzyme responsible for this production was shown to be peroxidase
(1 436a). Indeed, 'laboratory' lignin can be prepared by the carefully
controlled addition of dilute solutions of peroxidase and HzO
z
to a
stirred solution of an appropriate mixture of cinnamyl alcohols (Geissman
and Grout, )969). However, it seems evident that only sorne of the
various isoperoxidases isolated from plants are able to catalyze these
reactions.
37 BIOCHEMISTRY
One may consider that peroxidases play a key role in the overall
process of lignin formation by
1. generating HzOz necessary for oxidation and polymerization of
cinnamyl alcohols (357, 488, 489, 808).
2. oxidizing cinnamyl alcohols to phenoxy radicals (525) with the
rapid formation of oligomers.
3. converting ferulic to diferulic acid, which can act as a hemicellulose
cross link (828a).
4. a) binding cinnamic acid to wall proteins or carbohydrates (1435,
1436, 1436a)
b) polymerizing cinnamyl alcohols in walls (Brown, 1961).
Formation of H
2
0
Z
by cel! walls and cinnamyl alcohols oxidation
Several factors appear to be of importance in the formation of
HzO by cell walls with respect to the lignification process (357, 488,
z
488a, 489, 518) :
1) A bound peroxidase catalyzes the formation of HzO at the expense
z
of NAD(P)H in a reaction that is stimulated by monophenols and
Mn
z
+. Similar reactions have also been reported for soluble peroxidases
(Akazawa and Conn, 1958; 647).
2) HzO formation involves the superoxide radical 0z- as an
z
intermediate of the above-mentioned system.
3) 0z- equilibrates in part with a second mechanism, again producing
HzO in a separate and peroxidase-independent system.
z
4) The electron donor NADH can be provided by a bound malate
dehydrogenase. In anal ogy to the known malate-oxalacetate shuttles,
the possibility of a similar mechanism across the plasmalemma has
38 PEROXIDASES 1970/1980
been discussed (488). By this means, cytoplasmic reducing equivalents
could be provided to the cell wall. Furthermore, the concomitant
removal of accumulating oxalacetate would positively affect the
unfavorable equilibrium. of this reaction. Eventually, malate
dehydrogenase is also part enzyme-NADH complex susceptible
to the attack of 0z- as discussed in the preceding Section.
The reactions outlined above are illustrated in Figure 10.
R'OH R'O....lignin
._
.' 2 2 ----0

2
ROH -"RO' Y2


_ r i
malate
dehydrogenase
WALL oxalo-
ma/ate
acetate t-
CYTOPLASM t
Fig. 10. Reactions generating hydrogen peroxide in higher plant cell wall (after Gross
el al., 489).
Stimulation of H
2
0
Z
production by monophenols (and coniferyl
alcohol) is apparently due to their inhibiting effect on the formation
of peroxidase Compound III (518) which appears as a blocker of HPz
formation. It can also be mentioned here that the myeloperoxidase
mediated H
Z
0
2
formation accompanying phagocytosis also was related
to its NADPH oxidase activity in leukocytes (998a, 1308). Similarly
the bactericidal activity of eosinophil peroxidase is seen through a
perturbation of the plasma membrane with a respiratory burst, in
which oxygen is converted to hydrogen peroxide (634, 635).
BIOCHEMISTRY 39
In comparison to previous theories on the origin of HzO
z
in cell
waIls, the scheme proposed here offers several advantages. For example,
the problems relatedto the transport of 'toxic' HzO
z
from cytoplasmatic
sources to the cell wall compartment would be eliminated. Further,
regulation of the lignification process would be facilitated, either by
producing HzO
z
only within the lignifying areas or by degrading HzO
z
in the non lignifying parts by a wall-associated catalase that has been
found in cell wall preparations (357). One also might visualize that
both ROH and R'OH in Figure 10 represent hydroxycinnamyl alcohols.
In this case, the operation of the entire reaction sequence would depend
largely on the availability of these lignin precursors. The aforementioned
appreciable stimulation of HzO
z
formation by coniferyl alcohol would
support this idea. In this context, it should be noted that it was possible
to polymerize coniferyl alcohol in vitro with this rather cornpIex system.
Moreover, an analogous formation of HzO
z
has been reported with
cell walls isolated from Forsythia xylem (448a). This result obtained
with an actively lignifying tissue lends further support to the conclusions
drawn above.
Three peroxidase isoenzyme groups found in cell walls of tobacco
were tested for their capacity to form Hz Oz (808). Isoenzyme-group
GI, located only in cell walls (GU and GIll are also found in protoplasts)
showed the highest Kapp-value for HzO
z
formation. The lowest Kapp
value, i.e. maximal HzOz-formation, was received for group GIll which
is ionically bound to cell wall. Stimulation of HzO
z
formation by
coniferyl alcohol was much more significant than by p-coumaryl and
sinapyl alcohol.
Gross' work (489) has been confirmed. Working with carnation
stems, Czaninski and Catesson (191) discovered a heavy reaction in
sieve plates after incubation in a medium containing DAB, malate,
NAD and cofactors (MnCl
z
and p-coumaric acid) as weil as in a
medium containing only DAB and cofactors, i.e., in absence of exogenous
HzO
z
. The fact that endogenous H 0 may be locally produced to start
2 Z
the reaction is suggested by inhibition by catalase. On the other hand,
phloem cell wall peroxidases were found to have no affinity towards
cinnamic substrates except in differentiating and lignifying fibers. FinaIly,
peroxidases reacting with syringaldazine can be localized in lignifying
walls only (192).
::;.
40 PEROXIDASES 1970/1980
Ferulic ta diferulic acids. Binding ta wall carbahydrate and pratein
Diferulic acid, bound by ester linkages, has been identified in smal1
amounts in water-insoluble pentosans (arabinoxylans) of wheat
endosperm (828a) and in cell walls of Lalium (Hartley and Jones,
1976). Ferulic acid and diferulic acid are found in the ratio of 5: 1.
The coupling of ferulic acid side groups, attached to arabinoxylan
chains occurs through an oxidative phenolic coupling in which peroxidase
is involved as il1ustrated in the following scheme (828a)
-o-oMe M-o-eo 0
Arabino- Il Il r i
-O-C-CH=CH If OH + HO r; CH=CH-C-o-{A abno
xy
1
an } _ _ xylan
l Peroxidase H2 2
MeC
0_[ Arabino-
H xylan
Arabino- - J OH
xylan JI

OMe
Whitmore (1435) examined the capacity of soluble, ionical1y- and
covalently- bound peroxidase of slash pine callus and seedlings to
catalyze the binding of ferulic acid to cell wall carbohydrates. By using
caHus (which forms little lignin) and cambium cells from seedlings he
was able to show that the wall-bound peroxidases, particularly the
ionically-bound enzyme, catalyzed the coupling of ferulic acid to
carbohydrate most efficiently. With cambial cells phenol-phenol bindings
(as would be important in lignification) also occurred. In the same
way wall peroxidases catalyze the incorporation of dehydrogenation
polymer of coniferyl alcohol to wall protein containing hydroxyproline
during the early stages of lignification (1436, 1436a).
41 BIOCHEMISTRY
Polymerization
The studies begun nearly four decades aga by Freudenberg in
Germany have given us a much clearer idea of the nature of the
polymerization processes which constitute lignification in the truest
sense of the term. Freudenberg and Richtzenhain (1943) found that
press juice .from a cornmon mushroom, Psalliota campestris, contained
an enzyme system which could polymerize added coniferyl alcohol to
an amorphous product bearing a striking resemblance in both chemical
and physical properties to the natural lignin of conifers. It has since
been established that the enzyme responsible for this polymerization
is a phenol oxidase, laccase (Lyr, 1957; Freundenberg et al., 1958;
Higuchi, 1958), but it was still not completely clear at that time
whether the polymerization in higher plants was catalyzed chiefly by
laccase or by peroxidase (Lyr, 1957; Higuchi and Ito, 1958). A free
radical mechanism has been proposed (see Brown, 1961) for the
formation of these condensation products, in which the central
intermediate in the formation of coniferyl-type polymers is a quinone
methide, illustrated below :
00=C H - ~ H - C H 2 0 H
H
3
CO
Sorne evidence for the existence of such an intermediate has been
presented (Freudenberg et al., 1958). In a similar way the formation
of a quinone methide from the dimer could lead to molecules with a
higher degree of polymerization (Brown, 1961).
The three tobacco cell wall peroxidase isoenzyme-groups tested
before (808) for their capacity to form H
2
0
2
(and phenoxy radicals of
cinnamyl alcohols, see above) were also tested for their polymerization
capacity (807,808). Isoenzyme-group G l, located only in cell walls,
yield maximal polymerization rates for coniferyl and p-coumaryl alcohol.
G III (also found, in protoplasts) showed the lowest rates. The values
obtained for H
2
0
2
formation were opposite, thus pointing to possible
42 PEROXIDASES 197011980
different catalytic functions of the peroxidase isoenzyme-groups within
the il wall. As a result, Miider et al. (808) proposed a scheme of
lignification based on the different catalytic capacity of these peroxidase
isoenzyme groups (Fig. 11).
malate
malate
dehyd ragenase
oxala
acetate
Fig. II. Involvement of three different groups of wall peroxidases (G!, II and III) in
the lignification process (according to Miider et al., 808). .
OH R
RO#O OH f
B
OH R
1 1 - 1 -
"'" 1 1 OH
OH
C
"'" OH
H2
0
2
OR 0 OR 0 HO 8
Flayonol Choleon.
lpOO
H0'OQ=0
_ ,-dOH
-0-

:>.... 1 H02C f B OH

H02C) \;;d
o
Auronr a.nzoit acid Cinnamic acid
iPOO/H2 0 2

Q OH H0'r:0H HOQO
H02 C

OCH
3
1 1 1 + 1 1 POO 1
- R "'" OH:::"" 4:-:-=--"'" H
R 2 H2
0
2 H
o OH OH 0 OH 0
Flavanon.
Fig. 12. Involvement of peroxidases (POO) in catabolic pathways of fJavonoids in
plant cell cultures (after Barz and Nicolas, 1978).
H
2
0
2
lignins
Phenolics and extensin
BIOCHEMISTRY 43
No direct evidence is available to indicate that phenolics are indeed
cross-linked to extensin, although phenolics do occur in smaIl amounts
in cell walls. In this respect the catabolism of phenolics is often
overlooked. Barz and Nicolas (1978) indicated that peroxidases play
a very important role in oxidizing various flavonoids and aromatic
acids (Fig. 12). Zaprometov (1978) has also indicated that the lactonization
step in coumarin biosynthesis may take place with the formation of
free radicals generated through peroxidase. Many of these phenolics
are found in cell walls.
FinaIly, it is not clear whether the carbohydrate present in peroxidase
is there as a functional prosthetic group - in which case peroxidase
would have two prosthetic groups - or if the carbohydrate which was
added to the synthesized polypeptide, is simply there for transportation
out of the cell to become incorporated into the hemicellulosic fraction
of the cell wall, in the synthesis of which peroxidase plays a role.
Lignin degradation
Lignin degradation, namely by microorganisms, has been long
suspected to involve polyphenoloxidases such as peroxidase and laccase.
Based on multiple observations, a growing concept is being developed
that freely soluble peroxidase is not a lignolytic enzyme (529).
44 PEROXIDASES 1970/1980
2.3.4. Ethylene biosynthesis
The fonnation of ethy1ene during the degradation or peroxidation
of many kinds of organic mo1ecu1es has 1ed to extended studies of non
enzymic systems and the consideration that sorne of these mode1
systems might be operative in vivo (Osborne, 1978; 763a). Cu ions in
particu1ar induce a 1ight-driven peroxidation of membrane 1ipids 1eading
to ethy1ene fonnation (Sandmann and Bogger, 1980). As far as the
enzymatic synthesis of ethy1ene is concerned, on1y one substance is
known with certainty to be a precursor in vivo : L-methionine.
Methionine is converted enzymatically (by a transaminase) to cx-hydroxy
y-methy1thiobutyric acid and further to cx-keto-y-methylthiobutyric acid
(KMBA) and non-enzymatically (through the 1ight mediated action of
flavine mononucleotide FMN) to methiona1 (B
methy1thiopropiona1dehyde). In a further in vitro but enzymic system
consisting of precursor + peroxidase + cofactors, Ku et al. (1967, 1969)
found that both methiona1 and KMBA 1ed to ethy1ene fonnation (Fig.
13). Ana1yzing their enzymic system, Mapson and Warda1e (1968)
observed that next to peroxidase, a glucose-oxidase (generating peroxide)
and two cofactors, an ester of p-coumaric acid and methanesu1phinic
acid (Mapson and Mead, 1968; Mapson et al., 1969) were necessary
for the conversion of a cx-hydroxy-y-methy1thiobutyric acid or KMBA
to ethy1ene. These two latter substances, as weIl as methiona1, however
were inactive in (non-buffer) intracellu1ar conversion systems.
Yang (1968) also showed that ethylene is rapidly fonned from
methional or from KMBA by HRP in the presence of Mn
z
+, sot,
oxygen and a specific phenol (the active phenols include sorne
monophenols and rn-di phenols).
These two non-enzymic and peroxidase mediated ethylene generation
schemes present sorne similarities with the two possible mechanisms
of ethylene generation during host defense by neutrophils (neutrophil
is one of five types of leukocytes which circulate in the blood and
function as key elements in the defense of the host against invading
pathogenic organisms) (Tauber and Babior, 1977, 1978; Weiss et al.,
1977). The best characterized oxygen-requiring bactericidal mechanism
in neutrophils is the myeloperoxidase-dependent system, in which
myeloperoxidase mediates bacterial killing in the presence of HzO and
z
45 BIOCHEMISTRY
CH,-5-CH
2
- CH2- CH (NH
2
l-COOH 1
(methionine)
.t
CH
3
-S-CH
2
-CH
2
-CH (OH )-COOH
(O(. - hydroxy- K- methylthiobutyrie aeid)
~
CH
3
-S-C H
2
- CH
2
-CO- COOH CH
3
-S-CH
2
- CH
2
- CHa
(0(- k e t o - ~ - methylthiobutyrie aeid, KMBA) (methional)
0(.- D- glucose + glucose oxidase .... H
2
~
(H
2
0
2
) + peroxidase
{
P- cournarie ester
+ 1+ eofadors
methanesulphinie aeid
CH2 = CH
2
\0
:r
o
"'
(ethylene)
+
CH
3
-S-S-CH
3
(methyl disul fide )
+
HCOOH
(formie acid)
Fig 13. Alternative pathways of ethylene biosynthesis from methionine.
46 PEROXIDASES 1970/1980
a halide ion (probably C l ~ in the intact neutrophil). The H,O, used
by this system arises by the dismutation of 0,-, the product -of an
enzyme-catalyzed reaction in which NADPH reduces oxygen by one
electron. The O,--forming system is dormant in resting cells, but is
activated on exposure of the ceIls to suitable stimuli; the changes in
oxygen metabolism that result from the activation of this system are
designated the 'respiratory burst'. It was later shown that stimulated
neutrophils produce the highly reactive oxidizing hydroxyl radical OH",
which releases ethylene from methional (scheme beJow), and that the
O- generated during the respiratory burst is involved in the production
2
of this reactive species :
H 0 + O - ~ OH" + OH- + O
2 2 2 2
CH S - CH
2
- CH
2
- CHO + OH"--. CH S+ - CH - CHO + OH
3 3 2
CH $'" - CH - CH - CHO + O H ~ 1/2 (CH S)2+ HCOOH + CH = CH
2 3 2 2 3 2
The production of ethylene from methionine by Fentom's reagent (Fe-++
plus H,O,), a weil characterized source of OH", lends further support
to the cliim that methional is oxidized to ethylene by OH".
Two purified horseradish isozymes differing in their specific
peroxidase activity were tested as to their ethylene formation capacity
(Yang, 1968). Although the anionic A-I isozyme had higher specific
peroxidase activity (as measured by the peroxidation of o-dianisidine)
than the cationic C isozyme, C isozyme was about 250 times more
active (per unit peroxidase activity) than isozyme A-I in catalyzing
ethylene formation from methional. More recent labeling studies of
Adams and Yang (1979) provided evidence that ethylene was synthesized
in apple tissue from methionine via S-adenosyl-methionine (SAM, after
activation of methionine by ATP as the first reaction) and a 4-carbon
amino acid, l-aminocyclopropane-1 carboxylic acid (ACe), i.e. :
methionine ~ S A M --.ACC ---+ethylene. The conversion of ACC
to C
2
H
4
was inhibited by anaerobic atmosphere, free radical scavengers
and strong reducing agents. The reaction converting ACC to C
2
H
4
was
BIOCHEMISTRY 47
also inhibited strongly by various copper chelating agents (Apelbaum
et al., 1981), which suggests that a copper enzyme, possibly a copper
peroxidase, may be involved in the final step of C H biosynthesis.
2 4
The inhibitory phenomena are in accord with the known 02 requirements
for C H production (Lieberman, 1979), which now can be related to
2 4
the final reaction step from ACC to C
2
H
4

ln vivo peroxidase involvement ?
It is however doubtful if peroxidase is involved in the intracellular
conversion, for additions of catalase enhance, rather than reduce,
ethylene production, and endogenous peroxidase activity does not
parallel ethylene production (Kang et al., 1971).
The relationship of the peroxidative indoleacetic acid oxidase
system to in vivo ethylene synthesis in cotton was examined by Fowler
and Morgan (398). Modifications of peroxidase and IAA oxidase activity
in auxin-treated plants occurred weil after the elevation of internai
ethylene levels. This would indicate that the enzymes are not rate
limiting factors when ethylene synthesis is increased. It seems also
unlikely that peroxidase plays a role in producing C H from methionine
2 4
in the mungbean hypocotyl because chlorogenic or cafTeic acid, potent
inhibitors of peroxidase-catalyzed C H formation from methionine
2 4
analogs, did not inhibit C H production in this tissue even at 0.5
2 4
mM (Sakai and Imaseki, 1972). It can be argued that sorne isoperoxidases
only are concerned with the process. Considerable evidence indeed
now links the rates of ethylene production of growing or expanding
tissues with their levels of endogenous auxin and applications of auxin
to isolated plant parts invariably enhance the evolution of ethylene
(Osborne, 1978; Dubucq el al., 1978; Hofinger el al., 1980).
Since the specific activity of ethylene produced from C
4
C) methionine
was similar in control and auxin stimulated treatments, Sakai and
Imaseki (1972) concluded that the efTect of auxin was to stimulate the
enzyme system converting methionine to ethylene, and not to enhance
the formation of methionine. In addition, the Steen and Chadwick
(1973) proposai that auxin has two efTects on ethylene biosynthesis,
one immediate and cycloheximide-insensitive stimulation and a second,
48 PEROXIDASES 1970/1980
occurring after a lag period of 1-2 hr, which is sensItive to protein
synthesis inhibitors, has some striking paralle1ism with simi1ar immediate
and delayed auxin effects on activity and synthesis of specific peroxidases
(Ga1ston et al., 1968).
ACC can be converted to C H in model systems which invo1ve
2 4
an oxidation reaction requiring H)O) (Bolier et al., 1979; Lizada and
Yang, 1979). This suggests the possibi1ity of an in vivo peroxidase
system, which cou1d react with ACC to form C
2
H
4
Current1y, there
is no good evidence for such an in vivo reaction. However, the in vitro
system iso1ated from pea seed1ings by Konze and Kende (697a) suggests
such a system. Presumably, the enzyme could be present constitutive1y
in all tissues. It may be membrane-associated, for it did not survive
treatment with surface-active agents, and coId or osmotic shock reduced
the capacity of the system to convert ACC to C H Such treatments
2 4
will affect peroxidase binding to membrane (see Chapter 3).
There is also some striking resemblance between the stimulated
H)O)-dependent lignin synthesis and the increased ethylene synthesis
de -to the release and increased activity of the H
2
0
2
forming glucose
oxidase enzyme apparently attached to plant cell-wall material (and
liberated by the action of bacterial pectic enzymes as an example,
Lund and Mapson, 1970).
2.4. TYPES OF PEROXIDASES
Besides the higher plant peroxidases EC 1.11.1.7 which catalyze
the reactions mentioned in section 2.3.1, peroxidases from other sources
have been found with a particular affinity for specific substrates. Some
of them received a different code number in the enzyme nomenclature.
They are listed here below.
BfOCHEMfSTRY 49
Ascorbate peroxidase
L-ascorbic acid : hydrogen peroxide oxidoreductase
Ascorbate + H 0 = dehydroascorbate + 2 H 0
2 2 2
Other donors : pyrogallol, guaiacol, 1-:
Sources : higher plants, algae.
References: 673, 1207.
Bromoperoxidase (Bromide peroxidase)
Bromide : hydrogen peroxide oxidoreductase
p-hydroxybenzyl alcohol + Br-+ H,O, = 3-bromo-p-hydroxybenzyl alcohol
Ferriprotoporphyrin IX, glycoprteln.
Other donors : 1-: /
Sources : algae, marine invertebrates.
References: 7, 50, 1009.
Ch/oride peroxidase (Ch/oroperoxidase)
Chloride : hydrogen peroxidase oxidoreductase. EC 1.11.1.10.
2 RH + 2 CI- + H,O, =2 RCI + 2 H,O
Ferriprotoporphyrin x, glycoprotein. -
Other donors : I ~ Br-:
Sources : fungi.
References: 246, 505,1325, Morris and Hager (1966).
Cytochrome C peroxidase
Ferrocytochrome c : hydrogen peroxide oxidoreductase. EC 1.11.1.5.
Cytochrome c
2
+ + H,O, = cytochrome c
3
+
Ferriprotoporphyrin -IX.
Sources : aerobically grown yeast.
References: 170, 252, 328, 362, 363, 885, 941, 945, 1437.
50 PEROXIDASES 1970/1980
lodide peroxidase (/odopemr:idase)
lodide : hydrogen peroxide oxidoreductase. EC 1.11.1.8.
1- + H,O, + tyrosine = iodotyrosine + 2 HoO
21-+H,O,=I,+2H,O
Sources- : -thyroid, alg.
References : 915, 922.
Glutathione peroxidase
Glutathione : hydrogen peroxide oxidoreductase. EC 1.11.1.9.
Glutathione + ROOH = glutathione oxided
Selenium containing.
Sources : animaIs : mitochondria and cytoso!.
References: 474, 516, 783.
Lactoperoxidase
Donor : hydrogen peroxide oxidoreductase. EC 1.11.1. 7.
Its electron donor profile only difTers from that of plant peroxidases
regarding halide ions.
Derivative of mesoheme IX, glycoprotein.
Sources : milk, saliva.
References : 907, 1003, Hultquist and Morrison (1963).
Myeloperoxidase (Verdoperoxidase)
Donor : hydrogen peroxide oxidoreductase. EC 1.1 1.1.7.
Its electron donor profile only difTers from that of plant peroxidases
regarding halide ions.
Sources : leukocytes, macrophages.
References : 893, 965, 1123, 1308.
BIOCHEMISTRy 51
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For numbered references in the text, see bibliographical section
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FOX, L.R.; PURVES, W.K. 1968. The mechanism of peroxidase
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53 BIOCHEMISTRY
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54 PEROXIDASES 1970/1980
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BIOCHEMISTRY 55
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57 BIOCHEMISTRY
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58 PEROXIDASES 1970/1980
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BIOCHEMISTRy 59
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2
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2
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60 PEROXIDASES 1970/1980
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2
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YOKOTA, K.; YAMAZAKI, 1. 1965. Reaction of peroxidase with
reduced nicotinamide - adenine dinucleotide and reduced
nicotinamide - adenine dinucleotide phosphate. BIOCHIM.
BIOPHYS. ACTA. 105: 301-312.
ZAPROMETOV, M.N. 1978. Enzymology and regulation of the
synthesis of polyphenols in cultured cells. In 'FRONTIERS OF
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University of Calgary Press, Calgary, Canada, pp. 335-343.
CHAPTER 3
ISOPEROXIDASES :
FACT OR FICTION?
The large number of peroxidase 'isoforms' appearing in most plants
examined casts a certain amount of doubt as to them being native
molecules. The actual number obtained is dependent largely on the
separation techniques used (Brewbaker et al., 1968; 280; 584; 585;
738; 803). This, therefore, makes comparison of results from different
laboratories very difficult. Thus the non-initiated reader of a peroxidase
paper must be aware of the main factors causing this variation.
Buffer extractibility
The nature of the buffer used, its ionic strength, and its pH affect
the peroxidase recovery both quantitatively and qualitatively (Adatthody
and Racusen, 1967; Gaspar et al., 1969; 510; 796). Part of the
explanation certainly lies in the relative buffer solubilization capacity
for the (natural or artificiai) enzyme ionic association to cell organelles
and the wall. It certainly can be said that most peroxidase extractions
reported in papers dealing with plant physiological problems are imperfect.
62 PEROXIDASES 1970/1980
Extract manipulation, binding to organelles
The above statement also may explain the modifications in number,
intensity, size and aggregation properties, and migration speed of
peroxidases (304, 10 17, 1258) due to in vitro manipulations of the
extracts. Besides this differential release of cellular, intercellular and
organelle-bound peroxidases, the partial 'solubility' or 'pelletability' of
organelles indeed has to be taken into account in the crude or even
purified extracts. As an exemple, it has been demonstrated that
peroxidases appearing with an abnormally high molecular weight with
the peak of proteins after Sephadex (G-100 or G-200) filtration
(Cronenberger et al., 1966; Gaspar et al., 1969; Weber, 1970; 280,
610) were basic peroxidases apparently not different from those of the
second peak with a normal molecular weight : they simply had been
filtrated through Sephadex with the membrane structures on which
they were attached (282). Darimont and Baxter (279) state that such
membrane structures are still present in ribosomes and mitochondria
enriched preparations which renders the identification of the specifie
organelle-attached peroxidases uncertain. Peroxidases can be detached
from membrane structures in vitro and further reassociated with the
specifie aid of the calcium ion (1016).
It can be added also that the visualization of isoperoxidases in
gels is strongly influenced by the substrate concentration (Novacky and
Hampton, 1968), the pH of incubation and the hydrogen donor used
for the image enhancement (370, 651, 723).
Inhibitors, binding to phenolics, interconversion
The control of peroxidase activity through physical or chemical
factors may of course pass through repression or derepression of genes
leading to de novo synthesis (Galston et al., 1968; 1175) but it can
also be the result of activation of preformed inactive enzyme molecules
(Zucker, 1972) or mediated by non-protein effectors, mainly of a
ISOPEROXIDASES 63
phenolic nature (Gaspar, 1965; Dinant and Gaspar, 1967; 387, 619,
745, 1385, 1386). Peroxidase of Cichorium intybus is under the
photocontrol of phenolic inhibitors and sorne isoperoxidases submitted
to electrofocussing may migrate together with inhibitors (749). It is
possible that such an association exists in vivo (1002).
Following the disruption ofplant-cell organization, cellular phenolics
may be oxidized by phenol oxidase (Sheen and Calvert, 1969) or
peroxidase(Sheen, 1969) to quinones, condensed tannins, and ultimately
i':'
to brown pigments (Webb, 1966). Many examples are cited in the
literature showing that phenolics inhibit various enzymes during their
extraction from plant tissues (Anderson, 1966; Loomis and Battaile,
1966; Walker, 1980). A report from Fieldes and Tyson (387) suggested
a phenolic-peroxidase interaction during the extraction of the enzyme
from flax tissues. Data from Srivastava and Van Huystee (1257) suggest
that treatment with Dowex l-X l, which removes phenolics from
proteins, converts five anodic isoperoxidases into a single one. A same
result is obtained with albumin and cystein (1378). Along the same
line, Penel et al. (1017) found that a peroxidase from lentil root may
be transformed into several peaks after addition of a boiled extract.
As a general rule, it is advisable to remove phenolics from an extract
before the separation of peroxidases by electrophoresis. For this purpose,
many reducing or absorbent chemicals such as carbowax (1391), ascorbic
acid and/or cystein (499), insoluble polyvinylpyrollidone (Jones et al.,
1965; Castillo et al., 1981; 440, 510), collagen and casein dispersion
(500), etc., have been used. It is understandable, therefore, that the
physiological meaning of measurements made from such extracts is
subject to discussion. Effectors may have as an important regulatory
role as the enzyme activity per se. This seems to be particularly the
case for the so-called auxin-protectors (Rethore et al., 1974; Kevers
et al., 1981 a and b; 134, 137,436,955, 1305, 127, 1281).
Changes in number or properties of isoperoxidases have also been
reported fol1owing heat treatment (304), storage (1158), gel
chromatography at room temperature (616, 10 17) or incubation at
increasing pH (768). Recently, Decedue and Borchert (1980) claimed
that it is possible to convert the various isoperoxidases from potato
into a single electrophoretic species. This was obtained after
chromatography of potato juice in a column of Sephadex G-IOO. in
the presence of 2 M CaCI
2
"
64 PEROXIDASES 1970/1980
It thus appears from the literature that the numerous isoperoxidases
may be the product of interaction of a: few or even a single isoform
with other molecules. In addition, according to the method of separation,
the same biological material may exhibit a variable number of
isoperoxidases. For example, a separation of an extract from spinach
leaves yields nine bands after acrylamide gel electrophoresis, ten bands
with column isoelectric focusing, fifteen after isoelectric focusing in
acrylamide gel and up to sixteen bands after starch gel electrophoresis
(Pene!, 1976; 658). It was also reported that a single peak collected
after column isoelectric focusing may be resolved into several bands
by starch gel electrophoresis (Darimont, 1977).
Peroxidase-like activity
Other sources of misinterpretations have come from the state'ment
that peroxidase also display phenoloxidase activity and that other heme
containing molecules also catalyze the decomposition of hydrogen
peroxide and consequently the oxidation of classical peroxidase substrates
(Saunders et al., 1964). The apparent identity of polyphenoloxidases
and peroxidases revealed with sorne substrates has been discussed by
Van Loon (1393), who has developed a specific staining method
indicating non-identity with peroxidases.
Several isozymes from peanut cells in suspension medium however
possess peroxidase, IAA-oxidase and polyphenol oxidase activities (1255,
1257). The studies on the active site revealed that polyphenol oxidase
and IAA-oxidase share the same active site on the apoenzyme (1257).
Catalase is even able to function as IAA-oxidase (Avelia et al., 1966).
An additional source of error, when interpreting a peroxidase zymogram,
is the presence of cytochrome c which oxidizes guaiacol in the presence
of HzO
z
and shows three distinct bands of activity after starch gel
electrophoresis (434).
65 ISOPEROXIDASES
Cellular redistribution
Apparent absence of visible changes in peroxidases relative to
sorne particular phenomenon does not necessarily ref1ect the in vivo
situation. It has already been mentioned that possible release as soluble
peroxidases in the extracts of enzymes attached to organelles, by simple
ionic exchange due to buffers or by chelation, may occur. Fractionation
of extracts (with similar total enzyme activity) of different plants (133,
143, 1016, 1024) sometimes indicates a cellular redistribution of
peroxidases. This may or may not be associated with qualitative and
quantitative changes taking place in the course of sorne physiological
process. Thus, e.g., in vitro far-red and red irradiations of extracts of
spinach Ieaves modify the pelletability of peroxidase activity (\0\9).
These findings may render the comparison of results from different
sources more difficult and their interpretation doubtful.
Immunochemical and peptide mapping studies
In order to solve the problem of the existence of several distinct
forros of peroxidases, two techniques are feasible. The first one is the
immunochemical study of peroxidases. The second one is the comparison
of tryptic peptide maps or the elucidation of the complete amino-acid
sequence. There are only few reports concerning immunochemical
characteristic of peroxidase proteins. Bakardjieva and Georgiev (58)
showed that the peroxidase function in plants at different phylogenetic
positions may be realized by proteins differing in immunochemical
and serological properties. However, there is sorne antigenic similarity
among sorne plant species such as horseradish, pea, maize and barley,
but this similarity was not observed for aIl the peroxidase isoenzymes.
According to Cairns et al., (182) different peroxidase isoenzymes
from peanut Ieaves, peanut cells and peanut suspension cell medium
share cornmon antigenic deterroinants. There is also an immunological
relatedness between peanut and a horseradish peroxidase. These results
suggest an evolutionary conservatism in peroxidase structure. There is
however sorne reports on the distinct antigenic specificities of
66 PEROXIDASES 1970/1980
isoperoxidases in the same organism. Such data were reported by
Daussant el al. (287) in Datura stramonium and by Kahlem (645) in
Merclirialis annua.
The tryptic digestion of apoperoxidases gives peptides which can
be separated by two-dimensional electrophoresis. After staining, a
peptide map is obtained, which is characteristic of a protein. The
comparison of such maps is a mean of comparing the degree of
similarity between two proteins. This technique was used by several
authors. Shih et al. (1208) found that horseradish peroxidase isoenzymes
could be segregated into at least three distinct groups and it appeared
that there are many points of difference in the primary structure among
the three groups. In turnip root (1425), the two most acidic peroxidases
only differ significantly in one peptide and a third one is related to
these two. Horseradish isoperoxidase c also belongs to this group. But
the most cathodic peroxidase of turnip differs from this group, at least
around two disulfide bridges, and therefore, probably was different
from the other four in parts of its three dimensional structure. From
this study, it appears that each peroxidase contains two highly homologous
sequences.
In tobacco tissue culture eight isoperoxidases have been subjected
to trypsin digestion followed by peptide mapping. The peptide maps
of two of them were identical and ail the other isoperoxidases did not
appear to be dramatically dissimilar in certain portions oftheir sequence,
since many matching peptides were found when various isoperoxidases
were cross-compared. However, only two or three highly homologous
peptides were present in ail of the isoperoxidases. It therefore appears
that at least sorne portions of the peptides which include active sites
have been conserved among ail isoperoxidases from tobacco (680).
Tomato peroxidase can be resolved into two non-identical sub
units in the presence of dithiothreitol, while horseradish peroxidase
remains as a single polypeptide chain after such treatment (697).
Tobacco isoperoxidases G 1 were also unaffected by a similar treatment
(802).
It is thus difficult to know whether the numerous bands ofperoxidase
activity obtained by electrophoresis correspond to distinct proteins or
are conformers or degradative forms of one or two molecules. Much
work needs to be done in this area. Resolution of sorne of the above
problems will go a long way in establishing the structural authenticity
of isoperoxidases.
ISOPEROXIDASES 67
REFERENCES
For numbered reJerences in the text, see bibliographical section
ADATTHODY, K.K.; RACUSEN, D. 1967. On the extraction of
peroxidase isozymes from bean leaves. CAN. J. BOT. 45:
2237-2242.
ANDERSON, J.W. 1966. Extraction of enzymes and subcellular
organelles from plant tissues. PHYTOCHEM. 7: 1973-1988.
AVELLA, T.; DINANT, M.; GASPAR, Th. 1966. Action des acides
0-, m-, et p-hydroxybenzoiques sur la destruction de l'acide 13
indolylactique par la catalase de foie de boeuf. BULL. SOc.
ROY. Sc. LIEGE 35: 307-314.
BREWBAKER, J.L.; UPADHYA, M.D.; MAEKINEN, Y.;
MACDONALD, T. 1968. Isoenzyme polymorphism in flowering
plants. III. Gel electrophoretic methods and applications.
PHYSIOL. PLANT. 21: 930-940.
CASTILLO, F.J.; PENEL, c.; GASPAR, Th.; GREPPIN, H. 1981.
Masquage et dmasquage des isoperoxydases de Pelargonium.
C.R. ACAD. Sc. PARIS 292: 259-262.
CRONENBERGER, L.; VILLE, R.; PACHECO, H. 1966. Purification
partielle des auxine-oxydases des racines de Pisum sativum.
BULL. SOc. CHIM. BIOL. 48: 833-836.
DARIMONT, E. 1977. Les peroxydases de la racine de lentille.
Leur variation en rapport avec l'interaction auxine-cytokinine sur
la croissance. Thse de doctorat, Univ. Lige, 223 p.
DECEDUE, c.J.; BORCHERT, R. 1980. Potato peroxidase isozymes.
PLANT PHYSIOL. 65 (suppl.): 29.
DINANT, M.; GASPAR, Th. 1967. Acide 13-indolylactique-oxydase,
peroxydase, catalase, phnoloxydase et effecteurs naturels chez
Phaseolus vulgaris cultiv l'obscurit et la lumire. BULL.
SOc. ROY. BOT. BELG. 100: 73-94.
GALSTON, A. W.; LAVEE, S.; SIEGEL, B.Z. 1968. The induction
and repression of peroxidase isozymes by 3-indoleacetic acid. ln
'BIOCHEMISTRY AND PHYSIOLOGY OF PLANT GROWTH
SUBSTANCES'. Wightman, F.; Setterfield, G. (Eds). The Runge
Press, Ottawa, Canada, pp. 445-472.
68 PEROXIDASES 1970/1980
GASPAR, Th. 1965. Catabolisme auxinique et effecteurs auxines
oxydasiques. Etude compare chez Lens culinaris et Salvia
splendens. BULL. SOc. ROY. Sc. LIEGE 34: 391-537.
GASPAR, Th.; LACOPPE, J.; HOFINGER, M. 1969. Influence de
la nature, du pH et de la force ionique du tampon d'extraction
dans la mesure des activits peroxydasique et catalasique des
racines de Lentille. BULL. SOc. ROY. BOT. BELG. 103: 207-211.
JONES, J.O.; HULME, A.c.; WOOLTORTON, L.S.c. 1965. The
use of polyvinylpyrrolidone in the isolation of enzymes from
apple fruits. PHYTOCHEM. 4: 659-676.
KEVERS, c.; COUMANS, M.; DE GREEF, V.; HOFINGER, M.;
GASPAR, Th. 1981a. Habituation in sugarbeet callus: auxin
content, auxin protectors, peroxidase pattern and inhibitors.
PHYSIOL. PLANT. 51: 281-286.
KEVERS, c.; COU MANS, M.; DE GREEF, V.; JACOBS, M.;
GASPAR, Th. 1981 b. Organogenesis in habituated sugarbeet
calius: auxin content and protectors. Peroxidase pattern and
inhibitors. Z. PFLANZENPHYSIOL. 101: 79-87.
LOOMIS, W.D.; BATTAILE, J. 1966. Plant phenolic compounds
and the isolation of plant enzymes. PYHTOCHEM. 5: 423-438.
NOVACKY, A.; HAMPTON, R.E. 1968. The effect of substrate
concentration on the visualization of isoperoxidases in dise
electrophoresis. PHYTOCHEM. 7: 1143-1145.
PENEL, C. 1976. Activit peroxydasique et dveloppement chez
Spinacia oleracea. Thse de doctorat No. 1667, Univ. Genve,
160 p.
RETHORE, J.L.; GAS, G.; FALLOT, J. 1974. Les substances de
type 'protecteurs d'auxine' des explantats de parenchyme vasculaire
de Topinambour: libration et volution dans le milieu de
culture. C.R. ACAD. Sc. PARIS 279: 153-156.
SAUNDERS, B.C.; HOLMES-SIEDLE, A.G.; STARK, P.B. 1964.
Peroxidase. Butterworths, London, 27 J p.
SHEEN, S.J. 1969. The distribution of polyphenols, chlorogenic acid
oxidase and peroxidase in different plant parts of tobacco, Nicotiana
tabacum L. PHYTOCHEM. 8: 1839-1847.
SHEEN, S.J.; CALVERT, J. 1969. Studies on polyphenol content,
activities and isozymes of PPO and peroxidase during air curing
in three tobacco types. PLANT PHYSIOL. 44: 199-204.
: : ~ : : ~ ~ :
ISO PEROXIbASES 69
WALKER, J.R.L. 1980. Enzyme isolation from plants and the
phenolic problem. WHAT'S NEW IN PLANT PHYSIOL. 11:
33-36.
WEBB, J.L. 1966. Enzymes and metabolic inhibitors. ln
'QUINONES'. Webb, J.L. (Ed.). Academie Press, New York,
pp. 43 1-594.
WEBER, J.A. 1970. Sorne aspects of growth regulation in plants.
Ph.D. Thesis, Univ. Utrecht, 80 p.
ZUCKER, M. 1972. Light and enzymes. ANN. REV. PLANT
PHYSIOL. 23: 133-156.
.... ,
CHAPTER 4
PEROXIDASES AT
THE SUBCELLULAR LEVEL,
THEIR BIOSYNTHESIS AND
ITS REGULATION
4.1. CELLULAR LOCALIZATION OF PEROXIDASES
4.1.1. Technical aspects
Peroxidase activity is easily localized by light and electron
microscopy. The electron donor commonly used for this purpose is
3,3'-diamino-benzidine (DAB), which was introduced by Graham and
Karnovski (1966). Other reagents have been used; these include p
phenylene diamine (1065), benzidine (Van Duijn, 1955),
tetramethylbenzidine (866, 867), o-dianisidine (314), 3-amino-9-ethyl
carbazole (Graham et al., 1965), 2,5- or 2,7-fluorene-diamine (970)
and homovanillic acid (989). Syringaldazine has also been used, especially
to study the involvement of peroxidases in the process of lignification
(l90a, 191, 525). DAB, which gives a precise and strong staining
reaction appears to be the most suitable reagent for peroxidase staining
of tissues and ceIls. lt has the advantage that, in the presence of
hydrogen peroxide and peroxidases, it produces an osmiophilic polymer,
which is insoluble after post-fixation by osmium tetraoxide. The DAB
technique is very simple, but care must be taken to work under
72 PEROXIDASES 1970/1980
conditions (pH, temperature, H
2
0
2
concentration, percent aldehyde for
fixation) in which only peroxidases, and not other hemoproteins such
ascatalaseorcytochromescan react(376, 559,1118,1216,1289,1421).
The penetration of the staining medium is dependent on the
thickness of the tissue section. Incubation with thin sections allows
good penetration of the DAB reagents, but it leads to a considerable
loss of the enzyme into the medium (514). There is therefore a 10ss
of the activity. However, this loss can be reduced by a suitable
prefixation of the tissue with glutaraldehyde. Other possible sources
of artifacts should be mentioned. On one hand when organs or pieces
of tissue are cut, cellular redistribution of peroxidases may occur before
the fixation process is achieved, since mechanical injury can induce a
release of peroxidases out of cells. On the other hand, sorne peroxidases
are free in the cytoplasm (467) and in the walls and intercellular spaces
(see table 1). They can diffuse and be absorbed in a non specific manner
when cells are disrupted by cutting. Several isoperoxidases have a high
isoelectric point and can interact with negatively charged structures,
such as walls, membranes or ribosomes.
Despite these possible artifacts, which can lead to misleading
conclusions, cytochemical observations remain the best method of
studying cellular localization of peroxidases. Cell fractionation, the
other available method, give results which must be assessed with
extreme caution. The disruption of ceIls, indeed, mixes ail the cell
components and many non-specific interactions between peroxidases
and various cellular structures and molecules can occur. From this
point of view, reports on the presence of high peroxidase activity on
isolated ribosomes must be accepted with cautions (Matsushita and
Ibuki, 1960; 279, 1028).
In the same way, the level of peroxidase activity ionically-bound
to wall material in extracts, which is sometimes presented as having
a physiological meaning, is probably in part a reflection of the capacity
of cell walls to absorb solubilized peroxidases. There is however an
alternative technique available if one wishes to quantify the peroxidase
activity actually present in the wall and in the intercellular spaces.
This is the vacuum infiltration of a liquid into the plant tissue, followed
by the recovery of the fluid by centrifugation. This method was
introduced by Abeles and Leather (1971) and was applied to peroxidases
by Stafford and Bravinder-Bree (1262) (see also Castillo et al., 1981;
115, 153, 801, 870, 1077). This method, which does not affect the
73 LOCALIZATIaN AND BIOSYNTHESIS
protoplasts (protoplasts means here cells without wall in situ) has the
additional advantage that the ionic strength of the infiltration medium
can be chosen in such a way as to withdraw either free or ionically
bound peroxidases from the tissues. This was done by Miider (801)
who found three distinct groups of isoperoxidases present in the wall :
one which moves freely and can be extracted with water, a second
one ionically-bound and a third one which is covalently-bound. This
technique may also provide valuable information on the rate of release
of peroxidases out ofthe protoplast in relation to any chosen physiological
process (153).
As far as peroxidases of the isolated protoplast are concemed, it
is possible to separate the enzymes enclosed in a membranous structure,
provided that an appropriate extraction technique is used (mild grinding,
high osmolarity of the extraction buffer). This has been done for
vacuolar peroxidases (486).
4.1.2. Cellular localization
It is useful to keep in mind all the technical reservations mentioned
above when considering results conceming the cellular localizations of
peroxidases. Table 1 summarizes the various plant cell parts which
have been reported to exhibit sorne peroxidase activity. This is by no
way an exhaustive list orthe papers that have appeared on this subject.
Several questions arise when interpreting the numerous locations
of peroxidases at the cellular level. Is it possible that such reactive
enzymes are so widely distributed within plant cells ? Do artifacts
play a part in this distribution? It is not easy to answer these questions.
The presence of peroxidase in the cell wall is not a matter of
controversy. Cytochemical observations and vacuum infiltration of
(active) tissues provide sufficient evidence that cells release peroxidases
towards the extracellular spaces and that these enzymes remain active.
There are also indications that wall peroxidases partially differ from
protoplast peroxidases (153, 801). The existence of extracellular
peroxidases is also demonstrated in cell suspension cultures.
74 PEROXIDASES 1970/1980
More difficult to interpret is the localization of peroxidases within
the cell. There is little doubt that they are present in cistemae and
vesic1es of the Golgi apparatus, in small and central vacuoles and in
the endoplasmic reticulum. These localizations are apparentJy not
artifacts, since in these cases, the reaction product of DAB oxidation
is localized inside the closed membranes. It should be noted however,
that cytochrome P450, which is associated with the endoplasmic
reticulum, can exhibit peroxidase activity (1091, 1092). Vacuole
peroxidases have been observed by cytochemical techniques and after
cell fractionation. For example, Grob and Matile (486) reported that
in horseradish root, over 70 percent of the peroxidase activity is
contained in central vacuoles. Other reports on the presence of peroxidase
on the plasmalemma, on ribosomes and on nuc1ear components should
be reevaluated for the reason that all these cell structures carry many
negative charges and could trap peroxidase which diffuse after tissue
cutting.
Mitochondria and chloroplasts sometimes have been reported to
contain appreciable amounts of peroxidase. These localizations were
observed after separation of the cell components by density gradient
centrifugation. Cytochemical studies do not confirm these Jocalizations
which probably are due to contamination of chloroplast or mitochondria
fractions with other cell components (Pleniscar et al.,1967).
The overall conc1usion which can be drawn from the available
literature is that peroxidase activity is mainly associated with the
endocellular membrane system and the cell wall. The consequence of
this localization concerning both the biosynthesis of the enzyme and
its possible physiological fractions will be discussed later. However, it
is evident that every localization, revealed in the presence of exogenously
supplied hydrogen peroxide, does not necessarily correspond to a site
where peroxidases exert their function in vivo. Endogenous hydrogen
peroxide most likely acts as a limiting factor which can control to
sorne extent peroxidase activity.
The cellular localization of peroxidase has been intensively studied
also in animal celIs, especially in sorne specialized mammalian cells.
Peroxidases have been found in parotid and submaxillary glands (560,
957, 1296), in lacrimal glands (561: 562), in mammary glands (28),
in uterine epithelium (227, 794). AlI these organs have in common
the property of secreting fluid, in which peroxidases are thought to
exert an antimicrobial role. In addition, peroxidases have been found
LOCALIZATION AND BlOSYNTHESIS 75
in leukocytes (381, 1291), eosinophils (634, 635, 873), heterophils (318)
and macrophages (1001), mamrnary tumor cells (316, 317, 341), thyroid
epithelial cells (272, 959), etc. In almost every case, a study of the
intracell ular localization of peroxidase with the aid of electron microscopy
showed the presence of these enzymes in the endoplasmic reticulurn
(often including the nuclear envelope), in elements of Golgi apparatus
and in secretory granules. These cellular localizations imply that
peroxidases are exportable proteins; however, in sorne cases (thyroid
or Kuppfer cells of rat liver) they have been shown to be integral
membrane proteins (375, 1080).
A comparison between plants and animaIs shows therefore a great
sirnilarity in the subcellular localization of peroxidases. As it is in the
case in animaIs, peroxidases do not appear in every plant cell type.
We may say that the localization of peroxidases in plants varies with
seasons (Czaninski and Catesson, 1969), with species, with the degree
of differentiation and that the subcellular distribution is different in
each tissue (Poux, 1969; 190a, 191).
For example, peroxidase staining is particularly strong in the root
cap, epidermis, inner cortex and pith in Pisum (Poux, 1969; 391,
392); in phloern and maturing xylem (514); in the epidermis, hypodermis,
endodermis and sorne parenchyrna cells of hypocotyls of e.g., Phaseolus
(\939); and in sieve and parenchyma cells of cotton (191). Sorne cells
appear devoid of peroxidase activity, e.g., the cortical band and xylem
tissue of Pisum root (391, 392). In fully-expanded spinach leaves
extracellular peroxidase seems to be mainly located in small vascular
tissues, as it is the case in the young leaves of Vanda (Alvarez and
King, 1969). In the same organ, e.g., a root, the subcellular localization
of peroxidase differs from tissue to tissue and in the same tissue from
cell to cell.
A source of error during the histo- and cytochemical study of
peroxidase in plants, which is never discussed by the authors, is the
presence of many inhibitors of peroxidase activity. These inhibitors,
mainly of a phenolic nature, are often shown to be capable of masking
the activity of peroxidase in plant extracts (436, 684). It can be assumed
that they also interfere with the peroxidase reaction during the staining
procedures and furthermore the phenolic content of each tissue is
probably different.
76 PEROXIDASES 1970/1980
Table 1: Localization of peroxidases in higher plant cells.
Techniques of detection
Compartments
Cell wall
Plasmalemma
Cytoplasm
Golgi
apparatus
Light or electron
microscopy
Van Fleet, 1959;
De Jong 1967;
Poux, 1969;
161, 188, 191, 514,
515,993,1065,
1399,1420, 1480
Poux, 1969;
191, 467, 1420
467
Poux, 1969;
110, 161, 191, 265,
467, 514, 1480
Cell fractionation
115, 134, 188, 283,
391, 392, 440, 496,
739,801,804,1109,
1262
739, 1023
739, 1442
Secretory 467, 1480
vacuoles
LOCALIZATION AND BIOSYNTHESIS 77
Small vacuoles Poux, 1969; 253
191, 265, 467, 514,
993, 1052, 1053
Central vacuole
and tonoplast
Rough endo
plasmic
reticulum
Bound
ribosomes
Free ribosomes
Chloroplasts
Chromosomes
Nucleoles
Poux, 1969;
110, 188, 265, 1420
Poux, 1969;
188, 191, 265, 467,
514, 544, 1420
467, 1480
191, 467
1065
1065
124, 486, 993,
994
1024
Matsushita and
Ibuki, 1960;
279, 428, 739,
919, 1028
613, 919
78 PEROXIDASES 1970/1980
It is also weil known that the peroxidase activity of a whole plant
or a plant organ may be resolved into several isoforms by electrophoresis
(see Chapter 3). The question that arises is whether an isoperoxidase
corresponds to a particular localization in the cell or is specifie to one
kind of cell. This problem is not yet resolved. Mader and coworkers
(804, 805, 806) showed that in tobacco tissue cultures a fast migrating
anodic isoperoxidase moves freely in the cell wall and intercellular
spaces and is not present in the naked protoplast, while the two other
groups of isoperoxidases (slow migrating anodic group and slow migrating
cathodic group) are mainly located in the protoplast, and are respectively
covalently and ionically-bound to the wall.
Histoimmunology was used by Kahlem (465) to localize three
isoperoxidases which were specifie for male flowers of Mercurialis
annua. For that purpose, the specifie isoperoxidases were purified and
injected into rabbits. The resulting serum was used to 10calize the
'male' isoenzyme and it was shown that this isoenzyme only occurred
in the stamen and particularly in sporogenous tissue and the tapetum.
This kind of approach would be very useful not only to precisely
localize each isoperoxidase within the tissue and even within the cell,
but also to study the biosynthesis of isoperoxidases as was done in
Mercurialis. The results obtained by immunodetection wouId be more
reliable than those obtained after cell fractionation.
LOCALIZATION AND BIOSYNTHESIS 79
4.2. BIOSYNTHESIS OF PEROXIDASES AND ITS
REGULATION
4.2.1. De novo synthesis or activation
Peroxidases were used as marker enzymes for the study of numerous
physiological processes, as weil as for testing the effect of several
chemical substances on plant cells. They also strongly respond to
changes in the environmental conditions, to infectious agents (virus,
bacteria, fungi), and to injuries. Ali these factors affect peroxidases
either by changing their activity (perhaps more correctly their measured
capacity) or by changing the number of isoforms which can be
discriminated by electrophoresis. The variation of activity results either
from an inactivation or activation of preexisting molecules, from a
change in the rate of synthesis of the enzymes, or from the transfer
of peroxidases from one cell compartment to another. Most studies
do not provide any information on this point, but only report on
changes of peroxidase activity measured in more or less crude extracts.
Before going through the various steps in the control of the level
of peroxidase activity in plants, it must be stated that the simple
measure of peroxidase activity in crude extracts often is a misleading
reflection of the actual number of peroxidase molecules really present
in the tissue before extraction. Plant ceIls, indeed, contain several
substances (phenolics and others) which modify the ability of peroxidases
to oxidize the electron donors generally used to detect their activity.
These compounds, which probably are separated from peroxidases in
whole ceIls as a result of different compartmentalization, are mixed
with the enzymes when cells are broken and interact with the enzymes
during the assay.
A striking example of this difficulty is provided by studies using
Pelargonium (Castillo et al., 1981). Leaves or petioles of this plant,
when ground in a buffer according to the procedures commonly used
for the extraction of peroxidases, do not exhibit any peroxidase activity
as shown previously (Lavee and Galston, 1968; 436). However, the
conclusion that this organ fails to contain peroxidase is not correct,
80 PEROXIDASES 1970/1980
since the intercellular fluid collected by centrifugation after vacuum
infiltration exhibits very strong peroxidase activity. In this case it was
shown that the protoplast contained inhibiting and reducing substances
which, once mixed with the extracellu1ar peroxidase after grinding of
the organs, comp1etely mask this activity. This artefact can be overcome
by use of insoluble polyvinylpyrrolidone, which traps the phenolic
inhibitors (Jones et al., 1965).
It isevident from this examp1e that changes occurring in peroxidase
activity, fol1owing a change in the environment of cells, could be due
to the appearance or disappearance of inhibitors or activators. It could
also be due to a modification of transcription of RNA or of translation
of apoperoxidase. These steps can be studied by use of specific inhibitors
(Kanazawa et al., 1965; Gayler and Glasziou, 1968; Gahagan et al.,
1968; 954, 1108, 1190, 1315, 1381). Deuterium oxide used for density
labelling (Siegel and Galston, 1966; 30) or radioactively labelled amino
acids or sugars (1190, 1376) may a1so provide information about the
rate of peroxidase biosynthesis. Excised plant tissues are particularly
suitable for such studies. As a matter of fact, most tissues react to
injury or excision by an enhancement of their peroxidase activity
(Bastin, 1968).
4.2.2. Transcription
In sugar-cane stalk tissues (Gay1er and Glasziou, 1968) and excised
lentil embryonic axis (674), both 6-methylpurine and actinomycin D
reduce the increase of peroxidase activity which normally fol1ows
excision. By using these inhibitors and low temperature, the authors
were able to determine that the half-life for peroxidase rn-RNA decays
was 1.5 hour for sugar-cane and 3 hours for lentil. On the contrary
the stimulation of peroxidase activity in excised wheat embryos cultured
for 48 hours was not affected by actinomycin D, although the inhibition
of new RNA synthesis was effective (1315). This therefore indicates
that there may be conserved messengers for peroxidases, which are
capable of supporting peroxidase synthesis under conditions of strong
inhibition of RNA synthesis. The comparison between these two
examples shows that the life of messenger RNA for peroxidase may
be extreme1y variable.
81 LOCALIZATION AND BIOSYNTHESIS
This fact makes the study of the control of peroxidase synthesis
at the transcriptional level very difficult. The efTects of actinomycin
D were assayed in several systems. It was found to inhibit the peroxidase
stimulation induced by ethylene or injury in tobacco pith (115, 753),
sweet potato (Kanazawa et al., 1965, Gahagan et al., 1968), and pea
seedlings (1108). In cultured peanut cells, actinomycin D has an
inhibiting efTect only during a brief time following the lag phase of
growth (1381). But there are also several reports showing either no
efTect of this inhibitor (115) or even a stimulating efTect. The paradoxical
stimulation of peroxidase production was observed in oat leaves (954),
in potato roots (115) and in pea epicotyls (1108). In pea epicotyl
tissue, actinomycin D exerts its paradoxical efTect only when given
after ethylene. Ridge and Osborne (1108) suggested that it may enhance
the level of peroxidase by blocking the synthesis or the action of
specific inhibitors which inactivate the enzyme or prevent its translation
from a stable rn-RNA template. An alternative explanation would be
that actinomycin D induces a non-specific response at a post
transcriptional level.
4.2.3. Translation
ln contrast to actinomycin D efTects, inhibitors of protein synthesis
give unambiguous results when applied to plant tissue. However, in
one case, it was reported that cycloheximide enhances peroxidase
activity (1194). There are several examples showing that the stimulation
of peroxidase activity may be abolished by cycloheximide, blasticidin
S or other translation inhibitors. Ethylene (Gahagan et al., 1968; 1108),
injury (674, 1190), germination (1315), deetiolation (1194) and infection
(1371) are factors inducing a marked increase of peroxidase activity
which can be inhibited or diminished by such inhibitors. It is thus
likely that plant cells can control their peroxidase activity by changing
the rate of synthesis of peroxidase molecules. Another mode of control
may involve RNA as part of a repressor activity. Such a RNA fraction
is present in intact tobacco pith or in excised pith treated with IAA
(753). When applied to excised pith, it inhibits the appearance of the
new isoperoxidases due to excision.
82 PEROXIDASES 1970/1980
In peanut cell suspension, cycloheximide was shown to block
almost completely the synthesis of protein, but did not affect the rate
of peroxidase release into the medium (1382), suggesting the presence
of a large reserve pool of peroxidases either within the cell or in their
walls. In these cells, cycloheximide is active only after the transfer of
the cells into a fresh medium (1381).
Formation of rn-RNA and synthesis of the apoprotein are two
important steps in the control of peroxidase activity, but an additional
key factor in this control couId be the availability of heme within the
cell (1380). This availability is dependent upon porphyrin metabolism
and the synthesis of other porphyrin containing molecules, such as
chlorophyll and cytochromes.
4.2.4. Post-translational steps and secretion
There are further steps in the control of peroxidase activity. These
post-translational controis are likely to involve severai cations. Although
no clear demonstration has been made, the existence of peroxidases
in an inactive state was sometimes postulated. Recent data (Sticher
et al., 1981) showed that spinach celis, cultured in the absence of
calcium, contained peroxidases which could be activated by calcium
at millimolar concentration. Calcium-activated peroxidases were also
found in Hevea root (454). It is also known that one or two calcium
ions are incorporated in the apoprotein moiety of horseradish peroxidases
and are absolutely necessary to the enzyme activity (531). In addition,
Fielding et al. (391) reported that cell wall peroxidases of pea roots
are considerably activatedd when sodium or potassium were added to
the assay medium.
Finally , the transport of peroxidases towards their actual site of
action may also be considered as a control of peroxidase activity by
cells. Cytochemical studies have shown that the final locations of
peroxidases are likely to be either cell wall and intercellular free spaces
or vacuoles. An appreciable amount of activity is often detected on
ribosomes bound to the endoplasmic reticulum, suggesting that they
are synthetized there. Peroxidase activity on bound ribosomes was
often observed in plant and animal cells, thus indicating that the
LOCALIZATION AND BIOSYNTHESIS 83
coenzyme is readily incorporated to the proteinic part of the enzyme.
These peroxidases probably are transported towards the vacuoles or
the cell wall, following two distinct routes. In addition, peroxidases
are glycoproteins. Using affinity chromatography with concanavalin A
Sepharose, Nessel and Miider (942) found that ail the isoperoxidases
extracted from tobacco cel1s contained carbohydrate groups. In contrast,
Van Huystee (1376) also using affinity chromatography found that
sorne perQxidases from peanut cel1s did not possess the specific sugars
required for an affinity with concanavalin A. Whether these peroxidases
contained other sugars than mannose or are precursors for those retained
on con A Sepharose was not determined by the author. In the latter
case, the absence of carbohydrate would mean that the incorporation
of the sugar residue occurred at a post-translational level, for example
in the Golgi apparatus. Lew and Shannon (757), working with sliced
root tissue of horseradish incubated in the presence of 3H-Ieucine and
14C-mannose, came to the conclusion that the synthesis of the peptide
portion of peroxidase was completed before the monosaccharide residues
were attached to the molecule.
In another study, Sevier and Shannon (l187a) have described a
glycosyl transferase from horseradish root tissue which catalyzes the
transfer of 2-acetamido-2-deoxy-D-glucose from 2-acetamido-2-deoxy
D-glucose to the isoenzyme C of horseradish peroxidase. This peroxidase
was previously treated with a glycosidase and is used as acceptor to
study the glycosylation of protein in plants. There is no information
available from the literature on -the composition of the peroxidases
which are bound to ribosomes. If these peroxidases are devoid of their
carbohydrate part, they are likely to be enzymes just formed on the
ribosomes. But if they are already glycosylated, the hypothesis of an
artifactual binding to ribosome, fol1owing cell disruption, would be
probable. The data obtained by Lew and Shannon (757) and by Van
Huystee (1376) suggest that the biosynthesis of peroxidases is quite
similar to the biosynthesis of glycoproteins in mammalian systems. In
addition, the biosynthesis and the processing of peroxidase molecules
within plant cells exhibit the main characteristics of the secretory
protein in animais (Palade, 1975).
We know from the work of Maccecchini, Rudin and Schatz (783a)
that the apoprotein of yeart cytochrome C peroxidase is made outside
the mitochondria as a larger precursor, which is then transported into
mitochondria and processed to its nature form in the absence of protein
84 PEROXIDASES 1970/1980
synthesis. Stephan and Van Huystee (1271) succeeded in obtaining in
vitro synthesis of peroxidases with either free or membrane-bound
ribosomes. The peptide obtained by the procedure had the same
antigenic properties as the extra-cellular cationic peroxidase, but it had
a slightly higher molecular weight. The authors concluded that the in
vitro synthetized protein contained a signal peptide characteristic of
secreted proteins. They also showed that the amount of peroxidases
synthetized in vitro on membrane-bound polysomes was about twice
as much as that on the free polysomes (Stephan and Van Huystee, 1981).
In cress root hairs, peroxidases seem to be synthetized in the
endoplasmic reticulum and within dictyosome cistemae, packaged and
transported in secretory vesicles and extruded into cell wall (1480).
Many mammalian cells, which elaborate and secrete peroxidases, contain
peroxidase activity in the same cell compartment (562, 957, 1114,
1296). Thus it may be assumed that sorne analogies exist between the
intracellular route of peroxidases in animal and plant cells. This route
1eads to the exocytosis of peroxidases. In animaIs, several stimuli
inducing this exocytosis are known, e.g., carbamylcholine in 1acrima1
glands (562), or calcium (1061).
In plants, too, severa1 factors causing peroxidase re1ease into the
cel1 wall are known. These include osmotic shock (1480), ethy1ene
(1109, 1110), and air pollution (Castillo, personal communication);
whi1e gibberellins, for instance, reduce the re1ease of peroxidases (414).
Peroxidase secretion in rat 1acrima1 glands was shown to be dependent
on the presence of extracellular calcium, as is often the case for
secretion processes (1061). Calcium was also recent1y shown to be
invo1ved in the secretion of peroxidases by spinach cell suspensions
(Sticher et al., 1981). In addition, it was reported that calcium has
the property to bind sorne specific isoperoxidases to unidentified
membranes in lenti1 roots (10 16) and in squash hypocoty1s (1024).
This latter property cou1d be re1ated to peroxidase migration within
the endomembrane system. Electron micrographs often show that
peroxidase activity is closely associated to the membrane structure.
The involvement of calcium in the control of the intracellular localization
of peroxidase appears to be crucial, though much work is still necessary
to understand it exactly. It therefore appears that calcium is likely to
control peroxidase activity within the ceIl at several levels: viz, activation
of preexisting enzyme molecules, fixation of sorne of these enzymes
to selected membranes, and re1ease of the enzymes out of the cell by
exocytosis.
85 LOCALIZATION AND BIOSYNTHESIS
Another line of evidence suggests that peroxidases are also present
in vacuoles, often in great quantities (124, 486). It appears that the
enzymes are associated with the tonoplast (467, 1420). Vacuole
membranes are considered as end-products of the endomembrane system,
arising either from the endoplasmic reticulum or from the Golgi
apparatus (Morr and MoIlenhauer, 1976). It is thus tempting to
speculate that peroxidases synthetized in the endoplasmic reticulum
migrate towards the vacuole(s) bound to membrane elements (993).
Another explanation of the massive presence of peroxidases within the
vacuoles can be found in the autophagy process characteristic of plant
vacuoles. By this phagocytosis process, vacuoles are able to engulf
cytoplasmic constituents such as portions of the endoplasmic reticulum,
ribosomes, Golgi vesic1es, etc. (Matile and Wiemken, 1976). Peroxidases
could weIl be incorporated into vacuoles during this transfer of material
from the cytoplasm.
REFERENCES
For numbered references in the text, see bibliographical section
ABELES, ER.; LEATHER, G.R. 1971. Abscission: control of
ceIlulase secretion by ethylene. PLANTA 97: 87-91.
ALVAREZ, M.R.; KING, 0.0. 1969. Peroxidase localization activity,
and isozyme patterns in the developing seedlings of Vanda
(Orchidaceae). AMER. J. BOT. 56: 180-186.
BASTIN M. 1968. Effect of wounding on the synthesis of phenols,
phenoloxidase, and peroxidase in the tuber tissue of Jerusalem
artichoke. CAN. J. BIOCHEM. 46: 1339-1343.
CASTILLO, EJ.; PENEL, c.; GASPAR, Th.; GREPPIN, H. 1981.
Masquage et dmasquage des isoperoxydases de Pelargonium.
c.R. ACAD. Sc. PARIS 292: 259-262.
86 PEROXIDASES 1970/1980
CZANINSKI, Y.; CATESSON, A.M. 1969. Localisation
ultrastructurale d'activits peroxydasiques dans les tissus
conducteurs vgtaux au cours du cycle annuel. J. MICROSC.
8: 875-888.
DE JONG, D.W. 1967. An investigation on the role of plant
peroxidases in cell wall development by the histochemical method.
J. HISTOCHEM. CYTOCHEM. 15: 335-346.
GAHAGAN, H.E.; HOLM, R.E.; ABELES, F.B. 1968. Effect of
ethylene on peroxidase activity. PHYSIOL. PLANT. 21:
1270-1279.
GAYLER, K.R.; GLASZIOU, K.T. 1968. Plant enzyme synthesis
decay of messenger RNA for peroxidase in sugar-cane stem tissue.
PHYTOCHEM. 7: 1247-1251.
GRAHAM, R.c.; KARNOWSKY, M.J. 1966. The early stages of
absorption of horseradish peroxidase in the proximal tubules of
mouse kidney. Ultrastructural cytochemistry by a new technique.
J. HISTOCHEM. CYTOCHEM. 14: 291-302.
GRAHAM, R.c.; LUNDHOLM, V.; KARNOWSKY, M.J. 1965.
Cytochemical demonstration of peroxidase activity with 3-amino
9-ethylcarbazole. J. HISTOCHEM. CYTOCHEM. 13: 150-152.
JONES, J.; HULME, AC.; WOOLTORTON, L.S.c. 1965. The use
of polyvinyl - pyrrolidone in the isolation of enzymes from apple
fruits. PHYTOCHEM. 4: 659-676.
KANAZAWA, Y.; SHICHI, H.; URITANI, 1. 1965. Biosynthesis
of peroxidases in sliced or black rot-infected sweet potato roots.
AGR. BIOL. CHEM. 29: 840-847.
LAVEE, S.; GALSTON, AW. 1968. Hormonal control of peroxidase
activity in cultured Pelargonium pith. AMER. J. BOT. 55: 890-893.
MATILE, P.; WIEMKEN, A 1976. Interactions between cytoplasm
and vacuole. In 'TRANSPORT IN PLANTS III,
INTRACELLULAR INTERACTIONS AND TRANSPORT
PROCESSES'. Stocking, c.R.; Heber, U. (Eds.). Springer Verlag,
Berlin - Heidelberg - New York, pp. 255-287.
MATSUSHITA, S.; IBUKI, F. 1960. Peroxidase activity found in
the ribonucleoparticles from pea seedlings and rabbit liver.
BIOCHIM. BIOPHYS. ACTA 40: 540-542.
MORRE, D.J.; MOLLENHAUER, H.H. 1976. Interactions among
cytoplasm, endomembranes, and cell surfaces. In 'TRANSPORT
IN PLANTS III. INTRACELLULAR INTERACTIONS AND
TRANSPORT PROCESSES'. Stocking, c.R.; Heber, U. (Eds).
Springer Verlag, Berlin - Heidelberg - New York, pp. 288-344.
LOCALIZATION AND BIOSYNTHESIS 87
PALADE, G.E. 1975. Intracellular aspects of the process of protein
secretion. SCIENCE 189: 347-358.
PLENISCAR, M.; BONNER, W.D.; STOREY, B.T. 1967. Peroxidase
associated with higher plant mitochondria. PLANT PHYSIOL.
42: 366-370.
POUX, M. 1969. Localisation d'activits enzymatiques dans les
cellules du mristme radiculaire de Cucumis sativus L. Activit
peroxydasique. J. MICROSCOPIE 8: 855-866.
SIEGEL,B.Z.; GALSTON, A.W. 1966. Biosynthesis of deuterated
isoperoxidases in rye plants grown in O
2
. PROC. NATL.
ACAD. SCI. USA 56: 1040-1042.
STEPHAN, O.; VAN HUYSTEE, R.B. 1981. Sorne aspects of
peroxidase synthesis by cultured peanut cells.
Z. PFLANZENPHYSIOL. 10 1: 313-321.
STICHER, L.; PENEL, c.; GREPPIN, H. 1981. Calcium-requirement
for the secretion of peroxidases by plant cell suspensions.
J. CELL. SCI. 48: 345-353.
VAN DUIJN, P. 1955. An improved histochemical benzidine blue
peroxidase method and a note of the composition of the blue
reaction product. REC. TRAV. CHIM. 74: 771-778.
VAN FLEET, O.S. 1959. Analysis of the histochemical localization
of peroxidase related to the differentiation of plant tissues.
CAN. J. BOT. 37: 449-458.
CHAPTER 5
PHYSIOLOGICAL PROCESSES
MEDIATED BY PEROXIDASES
Peroxidases have been implicated in and associated directly or
indirectly with various physiological processes, including abscission,
aging and senescence, apical dominance, cold tolerance, dormancy,
fruit development and ripening, germination and early development,
irritation, reaction and resistance against parasitism, sex expression,
tuberization, etc. (see Subject lndex).
There are two major problems in trying to assign a particular role
for peroxidases in these different physiological events. First there is a
lack of genetically defined peroxidases in studies on growth and
development. Scandalios (1158) reports that defined peroxidase systems,
from a genetic point of view, are found in barley, maize and oats,
but we are not aware of the use of such information in developmental
studies. Second, by changing the conditions of the in vitro incubation
medium, it is possible to catalyze all the reactions mentioned above
by almost all types of peroxidases. Furthermore, there is relatively
little information conceming the cellular localization of the different
isozymes, the immediate environmental conditions for the manifestation
of their activity, or the specifie participation of each of them (if not
of sorne groups) in the physiological process being investigated.
Besides the possible but not specifie involvement of peroxidases
in many reactions, it would seem that, on the basis of available
evidence, isoperoxidases play four major roles in growth and development,
through their control and/or participation in :
90 PEROXIDASES 197011980
5.1. Auxin catabolism and consequently the endogenous free auxin level.
5.2. Lignin formation and cell wall biogenesis.
5.3. Defense mechanisms against pathogens.
5.4. Sorne respiratory processes.
The effects of light on peroxidases are examined in section 5.5.
5.1. AUXIN CATABOLISM
The involvement of peroxidase in general and of sorne more
defined isoforrns in particular in the control of endogenous auxin level,
and thus sorne physiological processes dependent on auxin, has come
from different in vitro investigations, the validity of which were
subsequently examined in vivo and/or in situ.
The most cornmon and direct evidence was the establishment of
a correlation between total peroxidase activity of a non-fractionated
extract, the capacity of the same to degrade IAA which is commonly
called 'IAA-oxidase' activity, in few cases (816a) the rough analysis
of the so-called endogenous auxin level (unfortunately measured through
biotests only until very recently), and the development of the physiological
phenomenon.
More indirect evidence has come from studies either on the effects
of exogenously applied positive (Mn
2
+, monosubstituted phenolics) or
negative (polyphenols) effectors of peroxidase as IAA-oxidase, or on
the endogenous variation of sorne of these effectors in relation to the
particular phase of the physiological phenomenon (Hare, 1964; Gaspar,
1965; Pilet and Gaspar, 1968). More refined correlations were established
91 PHYSIOLOGY
later after the fin ding by Mazza et al. (852) and Ricard and Job (lI 0 1)
that the more basic (cathodic) were the isoperoxidases, the higher was
their oxido-reduction potential against IAA and consequently their
capacity to destroy IAA in vitro (at acidic pH, in the absence of added
peroxides, thus essentially through their intermediary Compound III).
In several auxin-dependent physiological and developmental studies
there have been changes in fast moving cathodic isoperoxidases which
have been indirectly or directly correlated with the endogenous auxin
leveI. Below we give a few examples :
5.1.1. Cirovvth
In investigating maize dwarfism, Van Overkeek as far back as
1935 and 1938 showed that dwarf forms of this plant contained less
auxin than normal ones and that their extracts destroyed the
phytohormone at a higher rate. The higher peroxidase/IAA-oxidase
activity ofdwarf types was confirmed later for different plants (Kamerbeek,
1956; Chrometzka, 1958; McCune and Galston, 1959; Pilet and Collet,
1960; Gorter, 1961; Evans and Alldridge, 1965; 987, 1248). It was
shown for maize by Leyh et al. (1963) that this reduced activity of
dwarf forms could be attributed to a higher amount of inhibitors of
a phenolic nature (Bouillenne-Walrand et al., 1967).
Liang et al. (761) showed that a relationship existed between height
genes and peroxidase. They measured specifie peroxidase activity from
internode tissue of different height isogenic lines of sorghum. Tall
plants had less peroxidase per gram tissue than their short counterparts;
their FI offspring internodes were doser but had more peroxidase than
the tal1 parent. Peroxidase in the F
o
offspring was inversely related to
their height and followed a sim ply inherited pattern similar to that
for height. No such correlations were found between nitrate reductase
or acid phosphatase activities and height in these isogenic tines. The
authors conduded that peroxidase activity was not associated with
height by chance and that it probably had a functional relationship.
Similarly the association between plant height and peroxidase activity
92 PEROXIDASES 1970/1980
was found highly significant and negative in seven varieties of bread
wheat belonging to diverse genotypes, and their FI crosses (1230). The
lesser peroxidase activity in taller wheat varieties would result in the
accumulation or conservation of auxin which ultimately enhances the
growth.
Palmieri et al. (987) found that homogenates of tomato tissues
oxidized IAA at a rate proportional to their peroxidase activity. Two
monogenic recessive mutations were involved in the control of this
peroxidase activity. An inverse correlation was observed with two high
peroxidase mutants and leaflet size (length and weight) and their
epinastic and geotrophic-like behaviour. Enhancement of an organ
specific fast-moving cathodic isoperoxidase was observed in these mutants.
Galston and Davies (1969) in discussing genetic, hormonal and
environmental interactions in peroxidase/lAA oxidase activity presented
evidence (mostly from in vitro cultured tobacco pith) to suggest that
gibberellin, auxin, cytokinin and ethylene can interact to control the
level of peroxidase in the tissue. The auxin-cytokinin interaction on
growth has been shown to be correlated with their interaction on
specific cathodic isoperoxidases (450) resulting in the endogenous auxin
level control (Darimont et al., 1971). The spectacular growth effects
of exogenously applied gibberellin have been shown to be preceded
either by an increase in peroxidase/IAA oxidase polyphenolic inhibitors
(Galston and Warburg, 1959; Leyh et al., 1963) or by a depressing
effect on fast-moving cathodic isoperoxidases (1022, 1133). Gibberellic
acid promotion of expansion of spinach cells was similarly correlated
with a simultaneous suppression of peroxidase secretion in the culture
medium (414). These findings explained the sudden increase in
endogenous auxin after gibberellin treatements (Nitsch and Nitsch,
1959; Kuraishi and Muir, 1962; Gaspar and Bouillenne-Walrand,
1966). The gibberellin antagonistic effects of growth retardants like
CCC can be interpreted through their inverse action on the same
isoperoxidases (Lacoppe and Gaspar, 1968; Gaspar and Lacoppe, 1968;
428, 1133).
It must be mentioned that sorne data do not indicate any significant
effect of GA on peroxidase activity or anycorrelation with the auxin
destroying capacity of the tissues (879, 963) but these can be explained
on technical grounds, as resulting from the molarity of the buffer used
or the 'cell fractions analyzed (188). It was also found that CCC did
not affect specifical1y the isoperoxidase spectrum of wheat seedlings,
93 PHYSIOLOGY
but that microsomal-bound peroxidases were more abundant in extracts
of CCC-treated plants, and that CCC .interacted with the Ca-mediated
binding of peroxidases to membrane structures (133).
The inhibitory growth effects of light seem to depend also on the
variation of the activity of sorne peroxidases. In etiolated pea stems
the cofactor is kaempferol, which is present in low concentration.
Illumination of plants by red light increases kaempferol synthesis in
stems, which acts as a monosubstituted phenolic cofactor to increase
peroxidase/IAA oxidase activity and consequently leads to a decline
in stem growth (Mumford et al., 1961).
In cell suspension cultures of Phaseolus (38, 39) and of Si/ene
(747, 748) cultured on 2,4-0, drastic changes were observed in the
peroxidase zymograms during the growth cycle, i.e., total peroxidase
and IAA-oxidase activities decreased in parallel during exponential
growth and increased when growth rate was low. Old cells contained
isoperoxidases, found previously in the nutrient medium. The selective
release of isoperoxidases by young cells did not occur in senescent
cells (747, 748). Cytochemical studies also showed that the enzymes
were mainly cytoplasmic in young cells and mainly associated with
the wall in older cells (38).
Oevelopment of peroxidase/IAA oxidase isozymes was also
differentially associated with 2,4-0 growth promotion or inhibition in
Nicotiana (736), Daucus (180, 1445), Trigonella (60), Beta vulgaris
(Kevers et al., 1981a and b) and Arabidopsis (181, 938) callus tissues.
In these latter cases, 2,4-0 affected fast moving cathodic isoperoxidases
which once more indicates that it might act by altering the level of
endogenous natural auxins. Our feeling, based on the literature (1218)
and personal experimental data, is that most of the synthetic auxins
modify growth and other 'auxin'-dependent physiological processes by
this same mechanism.
The literature regarding the auxin dependence of so-called habituated
tissues has been reviewed in recent years (134, 690, 1305). The idea
that there is insufficient endogenous auxin for growth of normal auxin
requiring tissue in vitro was generally accepted although, due to technical
problems, very few valid auxin measurements (Syono and Furuya,
1972; Nischio et al., 1976) have been made. The controversial suggestion
that the rate of enzymatic inactivation of indoleacetic acid (lAA) is
higher in auxin-requiring tissues received sorne support from more
refined analyses of peroxidases (lAA-oxidase) isoenzymes and of their
94 PEROXIOASES 1970/1980
inhibitors, the so-called auxin-protectors (Stonier, 1970). However, such
a parallel analysis of peroxidase isozymes, auxin content and auxin
protectors had never been performed at the same time on auxin-requiring
and auxin-nonrequiring tissues of the same plant untiJ recently (Kevers
et al., 1981 a). A GC-ECO titration of IAA in normal auxin (2,4-0)
requiring and auxin-independent (habituated) sugarbeet callus revealed
an equal amount in both tissues. A comparison of the content and
pattern (through starch gel electrophoresis) of soluble, membrane and
wall peroxidases indicated that normal tissues contained a higher leve1'
of isoperoxidases. Normal tissues were also found to contain higher
levels of peroxidase inhibitors and auxin protectors (Kevers et al.,
1981 a). The hypothesized peroxidase-mediated higher rate of auxin
destruction in normal sugarbeet callus is supposed to be counterbalanced
by the 2,4-0-controlled auxin protectors. The invoJvement of inhibitors
of lAA-destruction in the process of induction for auxin-nonrequiring
calluses was confirmed by Syono (1305) and 2,4-0 control of auxin
protectors was further proved by Kevers (1981). Thus, an alternative
way of action of the synthetic auxins is via a more indirect control
of peroxidases through these auxin protectors, as has been shown to
be the case for gibberellin.
Senescence generally occurs after the cessation of growth and
inc1udes a series of processes leading to cell disorganization. Associated
with cell membrane disintegration (Winkenbach and Matile, 1970;
Matile and Winkenbach, 1971) and hydrolysis of ce]] wall polysaccharides
(Wiemken-Gehring et al., 1974), there is an increase in respiration
(see below). A plausible generalization of senescence (Mayak and
Halevy, 1980) is that it corresponds to a higher oxidation state of the
tissues, which may be in the form of accumulation of peroxides (Brennan
and Frenkel, 1977) or in lipoxygenase activity, resulting in iipid
hydroperoxides. This increase of peroxides and free radicals (Mishra
et al., 1976) is apparently related to an increased activity of peroxidases
in senescing petais at least (149; Carfatan and Oaussant, 1975; 1343).
Indeed, treatment of flowers with free radical scavengers delayed
senescence of carnation flowers (Baker et al., 1977). Gilbart and Sink
(1971) assigned to auxin a central role in the control of senescence in
poinsettia. The auxin level decreased in two poinsettia cultivars, but
it decreased faster in the short-lived cultivar. Also, the activity of IAA
oxidase and the level of hydrogen peroxide increased with aging.
95 PHYSIOLOGY
The above-mentioned increases in peroxidases, peroxides and free
radicals presumably were also involved in ethylene production (see
Section 2.3.4; Beauchamp and Fridovitch, 1970). On the other hand,
application of ethylene also enhances peroxidase activity (see Subject
Index) and catalyzes the synthesis of ethylene by plant tissues. This
phenomenon is cornmon to both jlower senescence (Mayak and Halevy,
19S0) and ripening of climateric fruits (1 136).
The function of increased peroxidase activity in fruit ripening has
also been examined (see Subject Index). Haard (496) found peroxidase
in both the soluble and residue fractions in pear, but the increase in
activity occurred in the particulate enzyme, and this was associated
with two isozymes not found in the soluble fraction. In this connection,
Ku et al. (70S) reported that during tomato ripening the threefold
increase in soluble peroxidase was associated with loss of one and
formation of three new isozymes. They suggested that the enzyme
might be involved in ethylene synthesis during ripening, although this
view is disputed (653). During ripening of mangoes the c1imacteric
and ethylene production were attended by a large increase in activity
of peroxidase and catalase, which was associated with the disappearance
of a heat-Iabile, non-dialyzable inhibitor of these enzymes (Mattoo and
Modi, 1969). An increase in these enzymes was also induced by
treatment of mango tissue slices with ethylene.
Auxin has been shown to retard ripening of banana (VendreII,
1969) and grape (Hale et al., 1970), and in the latter fruit endogenous
auxin declined at the time that ripening commenced. Since peroxidase
has the capacity for IAA breakdown, it couId provide a basis for
control of ripening, i.e., by destroying endogenous IAA and thereby
rendering the tissue sensitive to ethylene. Frenkel (399) investigated
isozymes of peroxidase and IAA oxidase in pear, tomato, and the non
c1imacteric blueberry and found an increase in from one to three
isozymes of IAA oxidase in each of the fruits during ripening, but he
found an increase in peroxidase isozymes only in pear and tomato.
He suggested that the increase in IAA oxidase in both c1imacteric and
non-climacteric fruits was consistent with the view that fruit ripening
is accompanied by an increase in capacity for auxin degradation, which
is necessary to make the fruit sensitive to ethylene.
This view agreed with the reports that grape ripening was initiated
by the disappearance of auxin (Coombe, 1960), and pear ripening was
inhibited by infiltration with auxin (Frenkel and Dyck, 1973). A more
1""" ""
\."
96 PEROXIDASES 1970/1980
detailed study of peroxidase variation as a function of storage time for
Golden Delicious apples (471) gave two peaks. The first peak
corresponded to c1imacteric and was apparently associated with
breakdown of hormones that retarded ripening. The second peak
corresponded to the start of senescence and couId we11 be a defense
mechanism against hydroperoxides. Peroxidase isoenzyme patterns were
similar during the ripening and senescence stages (125).
If there is any causal relation between the rise in peroxidase activity
and senescence, Birecka et al. (112) speculated that it might be mainly
related to elimination of H
2
0
2
, whose production in ce11s increased
with senescence. This could be physiologica11y important since a decrease
of catalase activity in senescing 1eaves has been often observed (e.g.,
Dhindsa et al., 1981). Thus, an increase in peroxidase activity wouId
represent an induced protective action, perhaps delaying senescence.
When senescence indeed starts in 1eaves there is increase in the
activity of peroxidase along with that of catalase (146, 221, 614). This
elevation in peroxidase activity corresponded to an increase in anodic
and cathodic peroxidases (167, 221, 659). Yellowing 1eaves with ethylene
also showed increased peroxidase activity (294).
Peroxidase activity has also been linked with the abscission of
leaves of cotton (894), bean (515, 1045, 1420), coleus (Sutcliffe et al.,
1969), tobacco (543, 546, 550, 554), citrus (442) and fruit of cherry
(1046, 1444). Both peroxidase activity and abscission are generally
enhanced by ethylene (Addicott, 1970; Beyer and Morgan, 1970; 1).
Part of this enhancement in enzyme activity could we11 be related to
the decrease in auxin level which has long been known to occur prior
to abscission in several systems (Addicott, 1970; Morgan and Durham,
1972; 442). Lignification through acidic peroxidases couId protect the
exposed scar (Addicott, 1970). The close correlation between the
increase in peroxidase activity and cell wall weakening may also suggest
an association with changes in hydroxyproline-rich proteins, which in
tum affect the extensibility characteristics of the walls, as mentioned
by Lamport (725) and Ridge and Osborne (1109, 1110).
97 PHYSIOLOGY
5.1.2. Morpho- and rganogenetic Processes
The so-called thigmomorphogenetic process (Jaffe, 1973) is
essentially a growth perturbation due to a mechanical stimulus. Rubbing
young intemodes of Bryonia dioica, which significantly decreased their
elongation, was followed by rapid changes in soluble and ionically
bound cell wall basic (cathodic) peroxidases, and with the appearance
of an additional isozyme (144). A decrease in the IAA level (quantified
by a GLC-ECD technique) in the intemodes was correlatively shown
(Hofinger et al., 1979). Pretreatment of the Bryonia plants with lithium
prevented the peroxidase changes (namely the appearance of the specific
isoperoxidase characteristic of rubbed plants) and the inhibition of
elongation due to rubbing (140). A similar relationship between a rapid
increase of activity of basic peroxidases and a mechanically induced
(by pricking) growth inhibition has been shown in Bidens pilosus plants
(Desbiez et al., 1981).
The dependence of the rooting and flowering processes on auxin,
if not their obligatory requirement for critical auxin levels, has been
discussed for a long time, but without any precise concepts until
recently. Absence of suitable techniques for IAA identification and
quantitation as weil as the absence of suitable biochemical markers
played important roles in the lack of precision. An intensive comparative
study of both processes using peroxidases of different plant materials
has considerably c1arified the apparently divergent situations (Gaspar,
1981; 444, 445) as indicated schematically in Figure 14.
An induction phase in the rooting process (in which no histological
events are observable) is characterized by a rise of the total peroxidase
activity of the whole cutting. Root primordia initiation takes place
following the peak ofactivity during a decrease of the basic isoperoxidases.
Flowering is associated with inverse variations of total enzyme activity
and basic isoperoxidases in inductive and initiative phases. Explants,
which have reached the rooting or flowering inductive phase on the
mother-plants can directly initiate root or flower primordia when
cultured in vitro. Considering that basic isoperoxidases are responsible
for the in vivo auxin catabolism, it has been hypothesized that rooting
and flowering are controlled by inverse variations of the auxin level
in their inductive as weil as their initiative phases (Fig. 14). Auxin
analyses and available literature data have supported this view (Gaspar,
198\). The following examples illustrate the working of this scheme.

98 PEROXlDASES 1970/1980
Spinach is a long day plant, which does not f10wer in short days.
However, after growth under short days for 1 month, f10wering is
rapidly induced in less than 24 hr, by transfer to long days or to
continuous light. lt can also be induced to f10wer under short days
by the application of GAl (Penel, 1976). Transfer to long days or
treatment with GA) leads to rapid dec1ine in cathodic peroxidases and
. ROOTING FLOWERING
PRE - INDUCED EX PLANTS

1
1
o
1
acidic p.
/'
1
basic p.
1
\.
1
1
NON -INDUCED EXPLANTs
acidic p. /' acidic p. )' acidic p. ~ 1 acidic p. ~
basic p. /'
basic p. \.
basic p. / _ ~ basic p. /
/
"
l
"
,
1
1 l '
1
/ 1
1
1 1
1
1

" i @ 1
1 1
1 1 1
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" 1
1 1
1 1
1
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DAYs
INDUCTION INITIATION INDUCTION INITIATION

]::
.:;:
acidic p. /' 1 11
basic p. .J'
~ /
DAYs
Qi
<Il
Cl
"0
X
o
....
Qi
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Ci
;
c
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1
Fif(. 14. Schematic representation of vanatIons in peroxidase (p.) and auxin levels
during the course of the inductive and initiative phases of rooting and
nowering by preinduced and non-induced explants (afier Gaspar, 1981).
99 PHYSIOLOGY
an increase in anodic peroxidases. After 48 hours there is a progressive
increase in cathodic peroxidases. Similarly during flower formation in
vitro in tobacco epidermal explants, there is a continuous increase in
fast moving cathodic isoperoxidases (1328). But this comparison could
only be made after having defined histologically that the transition of
the spinach meristem from the vegetative to the floral stage (479) was
taking place, and after having biochemically characterized tobacco
plants in their vegetative and the floral states, with respect to gradients
along their stem and floral axes (1328). Induction of flowering and
of other phytochrome-dependent processes could be obtained through
photomodulation and photodetermination of the same types of
peroxidases (1020, 1174, 1175).
During rooting of stem tips of Prunus (1063), of adventitious
shoots in Asparagus (1375), and of epidermal explants of tobacco (448,
1328) there is an increase in intensity of fast moving cathodic peroxidases
up to a maximum. This is fol1owed by a decrease in intensity, ail
prior to the morphological appearance of the roots. Knowing the
histology of these processes, Gaspar et al. (446) proposed that root
initiation involved at least two phases, viz: an induction phase in
which no histological events are observable, followed by an initiative
phase in which root primordium formation begins. These two phases
are marked with increased and then reduced peroxidasic activity and
a reverse relationship in auxin content, i.e., a decrease in endogenous
auxin fol1owed by an increase. This hypothesis can explain why phenolic
compounds such as ferulic and chlorogenic will inhibit rooting if
applied during the induction phase, and stimulate it during the initiation
phase as shown by Smith and Thorpe (1977). Compounds such as
these have been shown to interact with IAA oxidase and reduce the
rate of IAA oxidation (see Gaspar et al., 1964; Pilet and Gaspar,
1968). Recently Lee (740) has shown that the phenolic inhibitors
interfere with the first stage of IAA oxidation by preventing the IAA
. induced changes in the soret band of peroxidase. Apparently the
peroxidase is prevented from reacting with IAA to form the highly
reactive enzyme intermediates which lead to IAA degradation.
Variations in peroxidase and auxin levels during the course of de
novo vegetative bud formation appear to be different from the above
(Gaspar, 1981). De novo vegetative bud formation always occurs after
a prior increase of peroxidase activity in the expIant (Kevers et al.,
1981b; 448,569,745,750,800,806,927,938, 1131, 1327, 1328).
100 PEROXIDASES 1970/1980
Acidic as weIl as basic isoenzymes are involved. The curve drawn
from the results obtained with bud-forming epidermal layers of tobacco
(448, 1328) has been found to typically give the same lag and plateau
phases in the peroxidase activity evolution during bud formation as
has been observed in other materials such as chicory leaf explants
(745, 750), different tobacco systems including callus (800, 806, 1321,
1327), Arabidopsis (938) and sugarbeet (Kevers et al., 1981b). The
apparently obligatory tempory maintenance of the plateau before bud
,-" ..
i n i t i ~ t i o n appears specifically related to this organogenetic process.
IAA levels have been compared in different subcultures of
organogenetic and non-organogenetic habituated sugarbeet callus lines
(Kevers et al., 1981 b) during the exponential phase of growth. Results
indicated an average amount (+ or - 200 ng/g fresh weight) of the
organogenetic callus six times less than that (+ or - 1200 nglg fresh
weight) of the non-organogenetic one. Also an inverse relationship
between these IAA levels and the corresponding soluble peroxidase
activity (3.98 and 0.73 repectively) was obtained. This presumably
leads' to an auxin-cytokinin ratio suitable for the induction of shoot
formation (Skoog and Miller, 1975).
Similar indirect correlations between the peroxidase content, the
endogenous auxin level and embryogenesis in habituated shamouti
orange callus have been made. Embryogenic potential in ovular callus
is associated with a notably higher peroxidase activity and with the
appearance of an additional specific cathodic band (690). The same
dark-grown embryogenic callus was shown to decompose IAA at a
faster rate than non-embryogenic caHus (360). The embryogenic lines
could also deactivate IAA by conjugating it with aspartate faster than
non-embryogenic lines (1252).
Instead of considering the peroxidase mediation of physiological
processes through auxin catabolism by the simple auxin disappearance
two other explanations have been proposed and debated without final
conclusion at the moment (Skytt Andersen et al., 1972; Roberts, 1974;
372, 373). One concept is that the oxidation of IAA catalyzed by
peroxidase in plants yields products that stimulate growth (Tuli and
Moyed, 1969; Basu and Tuli, 1972; Frenkel et al., 1975; 870). Another
one considers the peroxidase auxin-oxidase complex as a system
generating inhibitory substances among which methyleneoxindole would
play the major role (Tuli and Moyed, 1967; Hofinger et al., 1980;
432, 438, 583).
PHYSIOLOGY 101
5.2. LIGNIN FORMATION
5.2.1. Growth
Fry's work (414, 415) has suggested that peroxidase restricted cell
extension and expansion by making the cell wall rigid in two ways :
a) covalently by catalyzing the conversion of feruloyl side-chains
into diferuloyl cross-links and
b) non-covalently by catalyzing the conversion of soluble phenolics
into hydrophobic quinones (or polymers).
GA
3
is hypothesized to prevent this process by inhibiting peroxidase
secretion (414).
Lignification is considered to be executed more specifically by the
involvement of acidic peroxidases (Nakamura and Nozu, 1967; 1445,
1447). It is quite interesting to note that this phenomenon seems to
take place immediately after breakdown of auxins, mediated by the
basic peroxidases. As an example, enhancement of anodic peroxidases
in rubbed young intemodes of Bryonia (144) occurred progressively
after variations of the cathodic ones. Old and already lignified intemodes,
which do not grow anymore, are characterized by high activity of these
same anodic peroxidases and they do not react to the mechanical stimulus.
Similarly, the cessation of elongation in Pisum sativum stems (424)
and growth reduction in camation plants after infection (Pugin et al.,
1979) had been attributed to a series of factors including peroxidase
mediated auxin-destruction, peroxidase-induced lignification and
extension-induced wall stiffening. These findings are probably related
to the parallel ethylene-mediated increase of wall hydroxyproline level
and activity of covalently-bound acid peroxidases (1109). Furthermore,
it has been shown that soluble (Shannon et al., 1966; 904) and at
least one of the three acidic covalently cell wall-bound peroxidases
(283) contained hydroxyproline.
These results are consistent with the often done observation that
the activity of ail types of peroxidases increases basipetally along with
growth cessating and lignifying intemodes (Macnicol, 1966; Mills and
Crowden, 1968; 144,425, 1328, 1375).
102 PEROXIDASES 1970/1980
Very interesting in this respect are the results of studies of Marigo
.(1979), who showed that tomato stem growth inhibition after root
feeding with lignin-precursors resulted from an increase in the lignin
cellulose ratio subsequent to a rise in the activity in the cell wall
bound peroxidases.
5.2.2. Differentiation - Vascularization
Usually, at the passage of the cells from a state of division to
elongation and, particularly, to differentiation, the total peroxidase
activity rises considerably. An investigation of four mutant genotypes
of Pisum sativum has shown an inverse relationship between peroxidase
activity and lignification of the pod membrane (138). From their
developmental studies, the authors suggested that peroxidase predisposed
cells to the lignification process per se : thus, cells in localized regions
wherein lignification subsequently occurred, i.e. those cells which had
become noticeably elongated, had a more intense peroxidase-staining
reaction than did the neighbouring non-differentiating cells.
The increase in peroxidase activity in cells from the pea epicotyledon,
which have ended their growth, would be due to an enhanced activity
of sorne of the present isozymes rather than to the appearance of new
ones (424). However, Sahulka (1141) found a peroxidase band in cells
from the zone of differentiation in a root of broad beans which is not
to be found in the zones of division and elongation. Upon the passage
of the cells from a state of division and elongation and differentiation
in germinating maize seeds,the increase of peroxidase activity is due
both to the appearance of new enzymes (mainly cathodic) and the
activation of s o m ~ e of the preexisting (namely anodic) isoenzymes (311).
That differe t isoperoxidases are associated with different types of
cell differentiatio , mostly through lignification, has been confirmed
by established corlrelations between a marked increase in enzyme activity
and the lignification of the seed integuments of Encyclia (Alvarez,
1968), vascularization (264, 488, 525, 564, 1453), and fiber formation
(499). Suberin contains a significant fraction of lignaceous materials.
103 PHYSIOLOGY
A high correlation between peroxidase activity and suberization was
observed. Peroxidase content of suberizing cel1s (after wounding in
potato) was more than 10 times higher than that of the immediately
adjacent dividing cells (127, 129).
The appearance ofnew peroxidase isozymes in peanut cell suspension
cultures was related to the cellular differentiation (1404). Varietal and
seasonal differences in lignification of pear sclereids are also dependent
on the association of peroxidase with cell walls (1074).
It has also been suggested that the continuous increase in activity
and number of fast moving anodic peroxidases in the course of root,
bud and flower formation was associated with a continued lignification
process for xylem cells differentiation in these newly formed organs
(445, 1328).
Contrary to lignification in aging tissues which seemed to be
preceded if not correlated with a decrease in the endogenous auxin
level, lignification in differentiating tissues couId be induced by increased
endogenous levels of IAA in these growing tissues. Differentiation
indeed was shown to be associated with the suppression of specifie
isoperoxidases working as IAA-oxidases (181,736,938,1113,1445).
5.3. DEFENSE MECHANISMS AGAINST PATHOGENS
Plants are able to provide active defense against pathogenic
organisms. Either, they are resistant, i.e., they prevent or restrict the
infection, or they are susceptible,i.e., infection develops, inducing host
damage. Peroxidases have been implicated in these two processes (Farkas
and Kiraly, 1958; Kosuge, (969). Stahmann and Demorest (1264,
1265) reported that in plants inoculated with selected viruses, bacteria
or fungi, there was a rapid increase in peroxidase and often the
appearance of new peroxidase isozymes. Sorne isozymes disappeared
104 PEROXIDASES 1970/1980
and new isozymes not seen in healthy plants appeared after pathogen
infection. Changes in isoperoxidase pattern following inoculation has
often been reported (483, 484, 1371). They may only affect one kind
of peroxidase (for example ionically-bound peroxidase). Reports showing
no changes in isoperoxidases are also available (1094).
Use of susceptible and resistant strains of cultivars generally have
shown that the latter immediately reacted to inoculation of an infectious
agent by an increase of peroxidase activity, while the former did not
exhibit this increase (1401) or reacted with delay to inoculation (1094).
Generally, resistant plants had a greater peroxidase activity than
susceptible plants before inoculation (1365). Beside natural resistance
to infection, resistance may be induced by a first infection or by a
chemical or physical agent. This acquired resistance was often correlated
with an increase of peroxidase activity. It has been reported to be
induced in tobacco Ieaves by prior injection of heat-killed cells of
Pseudomonas tabaci. Recently, Venere (1401) found no effect on
peroxidases when heat-killed Xanthomonas were injected to cotton
cotyledons, while living bacteria induced a strong increase.
Among the chemicals inducing peroxidase increase and resistance
development, ethylene is one of the most effective. Increased peroxidase
activity and resistance to black rot was found in sweet potato roots
incubated above infected roots in closed containers (Clare et al., 1966).
Apples, a source of ethylene, may replace infected roots in inducing
resistance. Ethephon, an ethylene precursor, also increased both the
resistance of susceptible tomato plants to Fusarium and their peroxidase
activity (1094). Ethylene, which could induce the release of peroxidases
by plant cells is known to be an element in the defense mechanism
(Paradies and Eistner, 1980). In tobacco leaves infected with tobacco
mosaic virus, a gradient of enhanced peroxidase activity from the lesion
edge to the tissue between the lesions was found (1430). In addition
to this localized reaction, several authors have observed the development
of a systemic induced resistance. This means that lesion formation in
lower Ieaves was followed by the appearance of resistance in upper
Ieaves, although the virus remained confined to the necrotic area.
Peroxidase activity increased in parallel with the development of
resistance of non-infected leaves (1121,1122, 1394, 1395). There is
therefore a large body of reports showing the positive correlation
between high peroxidase activity and resistance to pathogens (see also
Subject Index).
105 PHYSIOLOGY
Several functions may be attributed to peroxidases in relation to
the mechanisms of defense against infection. Lignification of diseased
tissue may be a mechanism of resistance (Vance et al., 1980). As
peroxidases are involved in lignin biosynthesis (see Section 2.3.3), the
increased peroxidase activity following pathogen inoculation may
intensify the formation of lignin. This hypothesis was confirmed by
Vance and coworkers (13 70, 13 71) who showed that cycloheximide,
which inhibited the resistance of canarygrass to Helminthosporium
averae, also blocked lignin biosynthesis and activity of enzymes involved
in lignin formation, including peroxidases. New formation of lignin
could prevent the penetration of the pathogen.
An alternative role of peroxidases in the resistance to viruses was
proposed by Simons and Ross (1122). They proposed that these enzymes
kill the infected cells, thus suppressing the multiplication of the virus.
However, it seems reasonable to think. that peroxidases are mainly
used by plants to attack pathogens. Two different mechanisms have
been proposed. The first one involved the production of oxidized
phenols arising by the action of wall peroxidases and phenoloxidase
(Kojima, 1931; 1366). Venere (1401) recently demonstrated that
peroxidase isolated from blight-resistant cotyledons formed a product,
which was bactericidal to Xanthomonas malvacearum, when incubated
in the presence of catechin and hydrogen peroxide. The production
of these two compounds was enhanced during infection. Peroxidases
also killed bacteria or fungi by another mechanism which was extensively
studied in animal systems. The myeloperoxidase or lactoperoxidase
hydrogen peroxide-halide system is known to have a strong antimicrobial
effect (Jago and Morrison, 1962; Klebanoff, 1967; 634, 100 1). The
white blood cells are able upon activation to produce all the elements
of this system, including hydrogenperoxide. It is tempting to draw a
parallel between plants and animaIs regarding the antimicrobial function
of peroxidases. Lehrer (1969) demonstrated that in the presence of
hydrogen peroxide and potassium iodide, human myeloperoxidase and
horseradish peroxidase were rapidly lethal for several species of fungi.
Southern bean mosaic virus was also irreversibly inactivated by exposure
to horseradish peroxidase, potassium iodide and hydrogen peroxide
(1366a). In addition, there is indication that during host-parasite
interactions, hydrogen peroxide production was enhanced (98 la). This
production of hydrogen peroxide is dependent on wall peroxidase (see
Section 2.3.3). The incorporation of iodide in organic compounds in
plants has also been established (Andr, 1973). Thus, the possibility
106 PEROXIDASES 1970/1980
exists that plants use the iodide-hydrogen peroxidase system to kill
parasites. Several phenols enhance the bactericidal effect of this system
(1366).
Despite ail the positive correlations existing between peroxidases
and plant resistance to pathogens, many authors have concluded that
peroxidases do not play an active role in the mechanism of defense
against infection. This conclusion is often based on the observation
that enhanced peroxidase does not always coincide with resistance. For
example, when inoculated with Puccinia graminis tritici, leaves of
resistant wheat kept at 20C exhibited an increase of peroxidase activity.
After transfer of this resistant plant with increased peroxidase activity
to 26C, reversion to a susceptible infection type occurred, but peroxidase
activity did not decrease during the reversion process (1180). Treatment
of susceptible lines of wheat with ethylene induced an increase of
peroxidase activity to levels above the activity exhibited by resistant
leaves, but treated leaves remained susceptible (271 a).
In tobacco, injection of leaves with sorne polyanions induced
resistance to mosaic virus and an increase of peroxidase activity, but
the two phenomena apparently were not related (1267). Increased
peroxidase activity was also observed in tobacco leaves infiltrated with
heat-killed bacteria, but this treatment only induced disease resistance
in leaves which were not kept in darkness. Similarly, increased peroxidase
activity was observed after treatment which did not induce resistance.
Nadolny and Sequeira (921) concluded from these data that the
peroxidase increase apparently parallels the development of disease
resistance and that peroxidases were not directly involved in protection.
Several points however are never discussed in papers concerning
l,,;'
the relation between peroxidases and the mechanisms of plant defense :
1) plants may react to pathogens by a release of peroxidases from cells
into intercellular spaces, without change in the total measurable
activity of the tissue;
2) the enzyme is one element of the peroxidase system and is only
active when hydrogen peroxide and phenols (catechin for example)
or halide is available.
These two facts could explain why resistance and increased peroxidase
activity are not always correlated. However, it is clear that plant
peroxidases certainly have bactericidal and fungicidal properties.
PHYSIOLOGY 107
5.4. RESPIRATION
In addition to the components of the tricarboxylic acid cycle, the
cytochrome and oxidative phosphorylation system, mitochondria
probably contain certain other oxidative enzymes (Nicholls, 1965;
Aylward and Haisman, 1969). Mitochondria from both animal (Neuberg
et al., 1962) and plant (Hackett and Ragland, 1962; Ivanova et al.,
1966) sources do indeed possess peroxidase activity which can be
resolved into a variable number of isoenzymes (279, 434). Rubin and
Ivanova (1963) showed that peroxidase can provide an alternate route
for oxidation of reduced nicotinamide adenine dinucleotide and it was
suggested (362) that one or more such mitochondrial peroxidases may
constitute a secondary pathway for electron transport without coupling
at the third site of oxidative phosphorylation. Further investigations
(1103) have revealed the presence of significant levels of peroxidase
and hydrogen donor to peroxidase in gradient-purified mitochondria
from mung bean hypocotyls. These could easily utilize any hydrogen
peroxide produced by the alternate oxidase pathway. Similar experiments
performed upon submitochondrial particles demonstrated a rate of
H10
1
production which could easily account for the net electron flux
through the alternate pathway. It is postulated (1103) that the alternate
pathway reduces oxygen partially to hydrogen peroxide, and that the
peroxidase (and catalase) activities of the mitochondria prevent its
accumulation.
A strong correlation has been shown to exist between peroxidase
activity and respiration rate during germination of rice. This finding
has led to peroxidase being considered as part of the respiratory
mechanism of the seedlings (999). It has also been observed in many
plants that peroxidase activity and respiration rate invariably increase
in parallel following infection (Rubin and Ivanova, 1958; 1390).
Several investigations have demonstrated that peroxidase activity
increased, with changes in its pattern, with the climacteric rise of fruits
(see 500). This has implicated peroxidase in the control of respiration.
Particulate peroxidase levels increase 3-fold with the initiation of the
respiration climacteric (496). However, these variations might be due
to differential phenol inhibition (500).
108 PEROXIDASES 1970/1980
5.5. LIGHT MEDIATED PROCESSES
5.5.1. Peroxidases as pigments
Peroxidases may be considered as pigments since they absorb
visible light. The question which naturally arises concerns the possibility
that light modifies the catalytic functions of peroxidases or even acts
on the physiology ofplants, in part, through its absorption by peroxidases.
No definite conclusion one way or the other can be drawn from the
literature. There have been many reports on the photochemistry of
hemoproteins; e.g., flash photolysis has been used to measure the
photodissociation of carbon monoxide complexes of hemoprotein
(Hasinoff, 1974). In addition, complexes of peroxidases with cyanide
were also found to be photosensitive (Keilin and Hartree, 1955). More
recent reports of Stillmann and coworkers (1275, 1276) have shown
that low energy polychromatic light of wavelengths between 320 and
450 nm can catalyze the conversion of HRP Compound 1 to Compound
II and Compound II to ferriperoxidase. These reactions occurred at
room temperature.
Earlier Sano (1147) had shown that upon aerobic oxidation of
IAA, HRP was converted to a verdotype substance having absorption
maxima at 405, 530 and 670 nm. This substance, designated P670,
when kept in darkness, was gradually converted into another substance
having absorption maxima at 403, 530 and 630 nm (P630). P630 was
reversibly returned to P670 upon light irradiation. Evidence indicated
that P630 and P670 had the same chromophore, a formylbiliverdine.
P630 was shown to be a complex containing carbon monoxide,
dissociable by light to yield P670. The author found that only specific
isoperoxidases were transformed into P670 and that P670-like compounds
were present in living tissues. The possible physiological significance
of these compounds remains to be elucidated.
109 PHYSIOLOGY
5.5.2. Peroxidases and phytochrome
A large number of enzyme activities are dramatically changed
during the de-etiolation of dark-grown seedlings (1175). This effect of
light is mediated by the chromoprotein, phytochrome. Phytochrome
exists under two forms with different absorption spectra. Etiolated dark
grown seedlings only contained P, the form having its maximum
- r
absorption at 660 nm. Vpon irradiation, up to 80 per cent of the
phytochrome molecules were converted to P
rr
, the form having its
maximum absorption at 730 nm. P the so-called active form of
rr
,
phytochrome, is responsible for the changes observed in enzymatic
activity. Red light, which increases P
rr
percentage has physiological
effects opposite to far-red light, which decreases Pre Operationally, an
enzyme regulated by phytochrome should react in an opposite way to
red and to far-red light (1175).
The regulation of peroxidase by phytochrome was described by
several authors (Mohr, 1972; 1175, 1237). Light often induces an
increase of peroxidase activity in etiolated seedlings. This was reported
in mustard cotyledons (1176), maize leaves (1194), bean hypocoty1
hook (292) and root and cotyledons of radish (592). The development
of extractable peroxidase activity in the mustard seedling was controlled
by phytochrome in an organ specific manner, i.e., enhancement in the
cotyledon and taproot, inhibition in the hypocotyl (1 I76). The same
specificity was observed in radish seedlings (592). Schopfer (l174a,
1175) made a distinction between modulation and determination as
modes of regulation in phytochrome-mediated photomorphogenesis. In
mustard cotyledon the response of peroxidases to light involved two
steps. In the first one, the response was induced by P
rr
while in the
second one the increase of peroxidase activity occurred. Schopfer
suggested that in the first light requiring step, inactive peroxidases were
synthetized and that in the second step these inactive enzymes became
activated by a process not involving PI;-. In contrast, the peroxidase
activity in etiolated maize leaves was photomodulated (1194). This
means that peroxidase activity increased as long as P,
Ir
was present. In
a series of papers Sharma and coworkers have reported that (i) the
regulation of peroxidase activity by phytochrome did not involve the
participation of kinetin, gibberellin, acetylcholine or c-AMP (1195),
(ii) that there was an age dependence of the phytochrome regulation
of peroxidase which mainly affected the 'soluble peroxidase' (1196),
(iii) that photosynthesis was not involved in this regulation (1197).
110 PEROXIDASES 1970/1980
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Fig 15. Effect of 2 min far red light on the actlvlty of a basic peroxidase activity
extracted from vertical leaves of spinach afi:er irradiation. The effect of light
is similar in directly illuminated (a) or in darkened (b) leaves (after Karege,
1981; Karege el al. 1982).
PHYSIOLOGY 111
As far as light-grown green plants are concerned little is known
about the possible relation existing between phytochrome and peroxidases.
- Actually, the physiology of phytochrome in non-etiolated plants is not
yet fully investigated. A peroxidase with, a basic isoelectric point,
extracted at high pH from spinach was shown to rapidly react to short
irradiations with red or far-red light (1019,1020). This peroxidase
activity underwent a fluctuation after an irradiation of 1 or 2 min
(Fig. 15a) and the shape of the fluctuations was dependent on the
light quality. An interesting fact concerning this effect was that the
photoconversion of phytochrome in sorne leaves of the plant immediately
modified the peroxidase activity in other leaves (Fig. 15b; 1021, 1026).
This implied the fast transmission of sorne signal from leaves to leaves
which was triggered by phytochrome photoconversion. This transmission
was inhibited by several substances including lithium chloride, EGTA
and the Ca
2
+ ionophore A23187 (Karege et al., 1982). Figure 16 shows
a mode! which accounted for the experimental data (1026) : the
transmission of the signal generated by phytochrome would result from
changes in K+ distribution; K+ changes would be correlated with
modification of cellular Ca
2
+ which itself controis peroxidase activity
distribution and/or synthesis within the cells. Red and far-red light
was also reported to affect peroxidase pelletability in extracts from
spinach leaves. This is possibly due to a different association of
peroxidases to the plasmalemma (1023). An effect of phytochrome
conversion in vitro was also demonstrated in membrane suspensions
of Cucurbita pepo (1025). ln that case, red and far-red light pulses
changed the peroxidase activity associated to membranes in an opposite
way.
The quality of light under which plants are grown seems to have
a great influence on peroxidase activity. In tomato leaves infected with
Septoria lycopersici peroxidase activity was greater under green and
red light and lower under orange and blue light (92, 93). ln spinach
leaves, peroxidase activity was greater under blue light than under red
light (Penel, 1976). In this latter case, no qualitative differences in the
isoperoxidase patterns were observed between blue- and red-light grown
spinach. The difference in total activity was due to cationic peroxidases
which were more active under blue light. Disks from leaves grown
under blue light also destroyed IAA more effectively than disks from
leaves grown under red light. This observation is in agreement with
the fact that spinach leaves are smaller under blue light.
112 PEROXIDASES 1970/1980
PLA N T
irrodioted leof non- irrodioted leof
! ---- 1. 1 1
peboes-stem ! 1
.C 0 \ ,', .... ------------------ ,
':0"''' ,,' K+
S
1 GNA L ",
ftK+ 'Q,o..o..

ll- . '
(c0
2
+ - --_ ...
C0
2
+
light
R/FR
Fig. 16. Tentative model to explain how light given to a leaf can induce changes in
peroxidase activity in that leaf as weil as in another leaf, kept in the dark
(after Penel et al. 1026).
Finally, germicidal ultraviolet light enhances peroxidase actlVlty
in detached bean leaves, inducing the appearance of two isoperoxidases.
The effect of uv is partially reversed by near-uv (SOl).
5.5.3. Photoperiodic control and flowering
The relative length of the day and night is a major element in
the determination of plant growth and development. Therefore, it can
be expected that peroxidases would be affected by photoperiod.
Unfortunately, there are only a few published studies on this aspect
of the regulation of peroxidases by light. Warner and Upadhya (1968)
showed that the shoot tips of Clementine tangerine and of trifoliate
113 PHYSIOLOGY
orange had higher peroxidase activity when grown under long days as
compared with short day-grown seedlings. In tobacco leaves, a group
of isoperoxidases which migrate slowly toward the anode was found
to become less active with increased day lengths (295). These two
reports appear to be contradictory. However, Parish (1969) has shown
that in wheat, light decreased the specific activity of peroxidase in
leaves and increased it in coleoptiles. One could reasonably expect
that light wouId have different effects on different organs, as it has
opposite effects on the growth rate.
A study with Cichorium leaf tissues showed that tissues cultured
in darkness have a greater peroxidase activity than those cultured under
light. Transfer of tissues from darkness to light induced a decreased
activity and vice-versa. Phenolics in light- and dark-grown leaves were
distributed in an inverse manner. This study leads to the conclusion
that peroxidase activity could be controlled by phenolic compounds
which primarily respond to light (746, 749). That phenolics vary
qualitatively and quantitatively on exposure to light is a well-established
fact (e.g., Engelsma, 1969). As an example, the oxidation of IAA by
peroxidases from Pharbitis cotyledons is strongly affected by the presence
of phenolic inhibitors. These inhibitors change according to the light
conditions and could be responsible for the differences in enzyme
activity observed (Konishi and Galston, 1964).
Peroxidase activity was extensively studied in relation to photoperiod
and floral induction in spinach, a long-day plant. As far as total
peroxidase activity is concemed, it appeared that young and old leaves
react differently to photoperiod. In young leaves, peroxidase activity
was stronger at the beginning of the short day than at the end, whereas
in old leaves the activity was stronger at the end (Penel, 1976).
In addition, the peroxidase activity followed a characteristic time
course during the life of the plant, reaching a minimum at the time
when spinach becomes induced to flower (658) (see also Section 5.1.2).
The floral induction was also characterized by a change in the balance
between acidic and basic isoperoxidases (1022). Particular attention
was paid to the basic isoperoxidases which responded rapidly to
phytochrome photoconversion, as mentioned earlier. The shape of the
fluctuation of this peroxidase activity, following a 2-minute irradiation
with red or far-red light, was different in vegetative or in induced
spinach leaves (660, 10 19, 1020). This difference could be used as a
quick test to discriminate induced from non-induced leaves, as the
114 PEROXIDASES 1970/1980
differences appeared weB before the onset of floral differentiation in
the shoot apex. The transition from the shape characteristic of non
induced spinach to the induced one occurred soon after the end of
the critical photoperiod, namely after 14 hours of light (660, 661).
Several physical or chemical factors which promoted or delayed floral
induction could be studied by using this peroxidase response as an
indicator (Karege, 1981).
In summary, it is therefore possible to explain many physiological
processes in the plant by involving specifie classes of peroxidases in
functions in which they have clearly been shown to be capable of in
vitro, and in many cases in vivo as weil. This role of peroxidases could
represent course control ofgrowth and development, in which peroxidases
respond to and interact with other factors such as phytohormones and
metabolites as a consequence of any perturbation in the environment.
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CHAPTER 6
L" .
PRACTICAL APPLICATIONS
OF PEROXIDASES
Since the paper of Peirce and Brewbaker (1010), reviewing the
applications of the analysis of isoforrns of difTerent enzyme systems,
proposais for the practical use of peroxidase as indicator of plant status
have increased.
Peroxidase electrophoresis is an efficient tool for large - scale
genetic investigations (1145) such as : identifying ramets, populations
or species hybrids, deterrnining the efTect of inbreeding and pollen
migration on the genetic structure of population and seed orchards;
or aiding breeding programs through indirect selection or through
development of breeding procedures.
Peroxidase electrophoresis has been proposed as an aid to
identification and phylogenetic studies of oat varieties or cultivars (22,
1226, 1469, 1470), Datura species (241), peanut cultivars (211), flax
genotypes and genotrophs (Tyson, 1969; 384, 385, 1353-1357), Nicotiana
species (Trinh et al., 1981; 574,1081,1201), Petunia and Poinsettia
cultivars (935, 1428), barley and wheat varieties (685-687, 1055), tulip
cultivars and their parrot mutants (1145), tomato species and mutants
(847, 1107), Aegi/ops species (1304), Oryza species (984), and several
plants at difTerent phylogenetic positions (53). Peroxidase isoenzymes
also served to characterize avocado cultivars, to document parentages,
and to detect outcrossing (1333-1335).
Although there is at present no conclusive proof that the isozyme
bands are direct gene products, it is evident that each genotype has
a recognizable isozyme pattern. The interspecific hybrids generally
show an additive pattern of parental peroxidases, which explains the
124 PEROXIDASES 1970/1980
weak activity or the absence of certain bands which are present in one
parent only (Trinh et al., 1981 ; 120 l, 1470). This apparently demonstrates
the mendelian inheritance of peroxidase isozymes, as originally suggested
by Hoess et al. (574) and confirmed by Snyder and Hamaker (1245).
Peroxidase can be used as a biochemical marker of sex expression.
Peroxidase activity is greater in gynoecious than in monoecious cucumber
plants while no differences were found in isoenzyme patterns (1095).
Specifie anodic peroxidases on the other hand constitute early markers
of staminal differentiation in Mercurialis annua (644-646). In both
types of plants however, the differences are connected with different
hormones levels, and hormonal treatments inducing changes in sex
expression also modify the enzyme status.
Data concerning specifie activities and isoperoxidase multiplicities
in relation to the ploidy status are relatively few (II, 338, 1043, 1158,
1251). In several varieties of beets and sugarbeets which differed in
ploidy level, significant differences were shown in the activity and in
the number of isoenzymes (Lobotskaya et al., 1968; Platon and Ciurea,
1969; 338). In sugarbeet, polyploidy induces a higher number of
isoenzymes for peroxidase but a lower number for esterase, acid
phosphatase and glutamic dehydrogenase (1251). Trinh et al. (1981)
working with the Nicotiana genus clearly shows an increasing gradient
in number and in intensity of the peroxidase bands from the hypohaploids
to the diploids. The previously mentioned qualitative differences (1081)
should be reevaluated since the absence of one band may simply be
due to the low concentration of the isoenzyme in the extract. It is
important to note (Trinh et al., 1981) that the ploidy-related differences
are only detectable when the same chronological and physiological
stages are taken into account. The most striking example of this is in
the case of the hypohaploids which develop aIl the bands present in
the haploids and diploids when increasing in age and remaining vegetative.
Results of peroxidase analyses in tomato plants (II) suggest that
the gene expression of the double gene dosage is enhanced in sorne
cases and depressed in others, resulting in a more unfavourable balance
of the metabolic processes. Furthermore using tomato mutants, Soressi
et al. (1248, 1249) concluded that the zymograms and total peroxidase
activities were not significantly correlated with a particular plant or
leaf trait. It may be inferred that mutations may influence directly or
indirectly the level of peroxidase activity without affecting the genes
which code for the peroxidase isozymes themselves.
PRACTICAL APPLICATIONS 125
In the Datura tetraploid, an isogenic and chromosomally 'balance
type', Smith and Conklin (1981) found no change from the diploid in
peroxidase activity. A genetic interpretation consistent with the resuIts
would be that the enhanced activity due to an increase in dosage of
the structural gene(s) is balanced by an increased production of
repressor(s) of gene activity, due to an increased dosage of regulatory
genes. This, together with the results of Trinh et al. (1981), shows
how difficult the interpretation of isozyme profiles can be, if factors
such as inheritance, ploidy leveland physiological state are not taken
into account.
We have mentioned earlier the role of peroxidase in fruit
development. Consequently, it has been considered as a possible
parameter of ripening and senescence (471).
A number of investigators have correlated the production of viny
or straw-Iike flavors to peroxidase activity. Arising from the studies
of Gardner et al. (1969), modification of peroxidase activity could thus
be a criterion of (loss of) quality in foods inadequately processed,
including corn products.
From the previously discussed relationship between peroxidase
(mainly cathodic forro), capacity of growth, and auxin availability for
growth, it has been suggested that peroxidase could have a possible
predictive value for sugarbeet. Peroxidase activity has been a suitable
parameter for establishing the degree of superiority among seedlings
of new sugarbeet hybrids, since a correlation was established between
the activity of the enzyme, the mean fresh weight and the sugar yield
(338, 435, 1251). A similar relationship of peroxidase activity with
grain weight has been established for different varieties of bread wheat
(1230).
Peroxidase has also been cited as a screening parameter for difJerent
physiological stresses. An elevated peroxidase Ievel is induced by cold
(Gerloff et al., 1967; Highkin, 1967; De Jong et al., 1968), drought
(Stutte and Todd, 1967; Viera-de-Silva, 1968), hypoxia (Siegel et al.,
1966) and salt stress (Strogonov, 1964; Rakova et al., 1969; 1273).
Peroxidase activity can also be taken as an indicator of diffrent
ion status (55, 98), deficiency (307, 1140) or toxicity (913) and as a
biochemical marker for different types of pollution (263, 395, 733,
811, 839, 1329). Plant peroxidases have often been used as a marker
for studying the response of plants to severaI air Fluoride
(Lee et al., 1966; 670, 672, 759, 1048), ozone (Dass and Weaver,
1968; 262, 263, 285, 359), S02 and N0
2
(579, 580), lead (811), zinc
(946) or gaseous HCI (359) were reported to have an effect on the
126 PEROXIDASES 1970/1980
level of peroxidase activity of several plant species. Peroxidases are
generally considered to be the most sensitive indicator of pollutants
in the absence of visible injury. The most commonly observed response
of peroxidases to poll,ution is an increase of their activity. In a few
cases, sorne effect on the isoperoxidase profile was reported (262, 263,
285, 811). Peroxidases have proven useful in determining areas where
plants were affected by F-containing exhausts of an aluminium smelter
(670). It was possible to detect hidden injury in several tree species
before the appearance of any visible symptom. Peroxidase activity also
allows one to measure the effect of pollution on plants in the vicinity
of a highway (395). It was also clearly established that in streets with
an intense motor traille, Sedum album leaves exhibited maximum
peroxidase activity when traille was maximum (l87a). In that case,
the time of the higher peroxidase activity was weIl correlated with the
time of higher concentration of air pollutants (CO, NO, S02)'
Increased peroxidase activity resulting from an exposure to pollutants
does not appear to be a general mIe. As an example, great differences
in peroxidase activity have been found in pine needles of 58 families
growing at differing distances from zinc-works (946). These different
reactions, which reduce the diagnostic value of peroxidase activity,
could be dependent on genetic characters. In addition, Endress et al.
(359) observed that peroxidase activity levels may be elevated by
subjecting plants to air pollutant stress. However, the activity was also
sensitive to the internaI physiological conditions of the plants. The
author came to the conclusion that due to its extreme sensitivity
peroxidase activity was not a reliable indicator of pollutant stress.
The reason why plant peroxidases are more active under pollution
is not known. Several comparisons may be made between the reaction
of peroxidases to pollution and to infection. For example, upon ozone
exposure, the peroxidase activity of an ozone-tolerant cultivar of soybean
is less affected than the activity of an ozone sensitive cultivar (263).
This may be compared to the differences observed between resistant
and susceptible plants (see Section 53). In the same way, peroxidase
reaction to air pollution often exhibits cornmon features with that
observed after infection (285, 482). Finally, plants already exposed to
a pollutant appear to be less responsive to a new exposure as compared
to plants coming from a non-polluted environment (580). This resembles
the acquired resistance following an infection.
PRACTICAL APPLICATIONS 127
In animaIs too peroxidase activity can be taken as an indicator
of pollution. As an example, effects of sorne industrial pollutants and
factory effluents on fish kidney peroxidase activity were recorded in
Ophicephalus punctatus and Clarias batrachus (911).
Extreme anodic and cathodic peroxidases have been involved both
in inductive and initiative processes of root formation (see Section
5.1.2). Thus it has been proposed (449) to use their respective activities
to select, from among different Asparagus plants, those individuals or
segments which are most likely to succeed in rooting on a defined
medium. The effectiveness of a prerooting treatment, as well as the
seasonal variation in rooting ability, can be monitored using peroxidases
as indicators. Thus these enzymes can be exploited as a sereening test
for difJerentiating the efficiency ofchemicals in the regulation of different
physiological processes.
These are a few examples of the potential practical exploitation
of peroxidase and its isozyme forms. On the basis of their participation
in various physiological processes, many others can be imagined. One
such possibility is the selection between disease resistant and susceptible
types (see Section 5.3). However, to date the potential diagnostic
application of peroxidases remains unfulfilled.
In addition to their applications in physiological and genetical
studies, peroxidases are widely used as tracers in neurology and for
the immunodetection of a great number of molecules. These two
subjects account for a great part of the papers dealing with peroxidases
but are not covered by the present book.
128 PEROXIDASES 1970/1980
REFERENCES
For numbered references in the text, see bibliographical section
DASS, H.C.; WEAVER, G.M. 1968. Modification of ozone damage
to Phaseolus vulgaris by antioxidants, thiols and sulfbydryl
reagents. CAN. J. PLANT SCI. 48: 569-574.
DE JONG, D.; OLSON, A.; HAWKER, K.; JANSEN, E. 1968.
Effect of cultivation temperature on peroxidase isozymes of plant
cells grown in suspension. PLANT PHYSIOL. 43: 841-844.
GARDNER, H.W.; INGLETT, G.E.; ANDERSON, RA. 1969.
Inactivation of peroxidase as a function of corn processing.
CEREAL CHEM. 46: 626-634.
GERLOFF, E.; STAHMANN, M.; SMITH, D. 1967. Soluble proteins
in Alfalfa roots as related to cold hardiness. PLANT PHYSIOL.
42: 895-899.
HIGHKIN, H.R 1967. Effect of temperature on formation of
peroxidase isozymes. PLANT PHYSIOL. SUPPL. 42: S 16.
LEE, c.J.; MILLER, G.W.; WELKIE, G.W. 1966. The effects of
hydrogen fluoride and wounding on respiratory enzymes in soybean
leaves. AIR WATER POLLUT. INT. J. 10: 169-181.
LOBOTSKAy A, L.; BYEKKO, Y.A.; PALCHENKO, L.A.;
BORMOTOV, V.Y. 1968. Action of peroxidase and respiration
intensity in sugar beet plants with different ploidy levels (in
Russian). DOKL. AKAD. NAUK. B. SSR 12: 563-565.
PLATON, M.; CIUREA, G. 1969. Etude physiologique de quelques
formes polyplodes roumaines de betterave sucrire.
REV. ROUM. BIOL. 14: 309-313.
RAKOVA, N.; KLYSHEV, L.; STROGONOV, B. 1969. The effect
of sodium sulfate and sodium chloride on the protein composition
of pea roots. FIZIOL. RAST. 16: 22-28.
SIEGEL, S.; GIUMARRO, c.; DALY, O. 1966. Micro-aerobic
capabilities in land plants: observations on survival and growth
of plants submerged in fresh and saline waters. NATURE 209:
1330-1334.
129 PRACTICAL APPLICATIONS
SMITH, H.H.; CONKLIN, M.E. 1981. Effects of gene dosage on
peroxidase isozymes in Datura stramonium trisomics. 3rd Int.
Conf. Isozymes. Markert, c.L. (Ed.). Academic Press, New York,
in press.
STROGONOV, B. 1964. Physiological Basis of Salt Tolerance in
Plants. ACADEMIC SCIENCE U.S.S.R. (Davey, New York).
STUTTE, c.A.; TODD, G. 1967. Effects of water stress on soluble
leaf proteins in Triticum aestivum L. PHYTON 24: 67-75.
TRINH, T.H.; GASPAR, Th.; TRAN THANH VAN, K.;
MARCOTTE, J.L. 1981. Genotype, ploidy and physio10gical
state in relation to isoperoxidases in Nicotiana. PHYSIOL.
PLANT. 53: 153-157.
TYSON, H. 1969. Peroxidase activity in Linum usitatissimum. L.
ANN. BOT. 33: 45-54.
VIERA-DE-SILVA, J. 1968. Le potentiel osmotique du milieu de
culture et l'activit soluble et latente de la phosphatase acide
dans le Gossypium thurberi. C.R. ACAD. Sc. PARIS 67: 729-732.
CHAPTER 7
CONCLUDING REMARKS
AND PROSPECTS
Peroxidases obviously are involved in many fundamental aspects
of animal and plant life. The present book is an attempt to relieve
their outstanding properties. They have been a little more c!arified
during these last years along with the refinement of the techniques
used for the study of their physico-chemical characteristics and their
physiological functions. Let us hope that more and more 'peroxidasers'
will help to the understanding of what was still until recently called
a true morass.
The peroxidases as a group need to be further defined in terms
of their genetics, physico-chemical properties, and physiological
significance. As already c!aimed by Scandalios (1150) for isozymes in
general, a precise definition of the basis for peroxidase multiplicity is
a necessary prerequisite to the understanding of the significance of
spatial and temporal isoperoxidase fluctuations encountered in plant
development. It is now obvious, and everybody must be aware, that
. the appearance or disappearance of isoperoxidases during development
or in the course of a physiological process does not a priori reflect
gene action in the sense of transcription. It does reflect the expression
of genetic information, however, and the regulation of such difTerential
gene activity can be at a number of control points, as discussed in
the preceding chapters.
In the immediate future, the most important questions relating to
the existence of multiple 'molecular' forms of peroxidase concern their
role in cellular metabolism and difTerentiation. Information as to their
biochemical and physiological functions came through the knowledge
! : : ~ ; : : : . : :
i ~ ~ t ~ ~ ~ ~ ~
132 PEROXIDASES 1970/1980
of the factors determining the basis of their subcellular distribution.
together with a thorough investigation of their physico-chemical
properties. Although catalytic functions may be similar, kinetic differences
may allow flexibility in biological role.
In many instances, peroxidases have proven useful as indicators
or markers of the reactions of plants to external stimuli such as light,
prickings, rubbings, infections or pollutions. Plants, as immobilized
and autotroph organisms, are tightly dependent upon the environmental
conditiOns. They must often adjust themselves very quickly to external
changes through elastic or plastic modulations of their functioning.
This reactivity cannot be achieved through sole long-term responses
involving protein synthesis, but requires immediate and quick regulation.
The former is linked to metabolite and hormone circulation, whil
the latter is linked to ion and electrochemical transport. Colloidal and
microtrabecular systems, as well as membranes, play an important role
in these short-term regulations, which often involve peroxidases.
Intercellular or interorganismic communications, which are required
in these processes, were in sorne cases visualized by rapid qualitative
or quantitative changes in peroxidase activity (142, 143, 1021). ~ T h i s
reactivity of peroxidases is an additional reason for a better understanding
of their regulation.
1
O M . ~ ~ H V d
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----
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peroxidase. Tryptic glycopeptide containing two histidine residues and a
disulfide bridge. FEBS LETT. 30: 243-245.
1424. WELINDER, K.G. 1976. Covalent structure of the glycoprotein horseradish
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1424a. WELINDER, K.G. 1979. Amino acid sequence studies of horse radish
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1426. WELINDER, K.G.; SMILLlE,
horseradish peroxidase. Il.
50: 63-90.
L.B. 1972. Amino acid sequence studies of
Therrnolytic peptides. CAN. J. BIOCHEM.
1427. WELINDER, K.G.; SMILLlE, L.B.; SCHONBAUM, G.R. 1972. Amino acid
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BIOCHEM. 50: 44-62.
1427a. WELLBURN, A.R.; CAPRON, T.M.; CHAN, H.-S.; HORSMAN, D.O. 1976.
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,-'-
250 PEROXIDASES 1970/1980
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252 PEROXIDASES 1970/1980
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1
. 1
1
1
AUTHORINDEX
ABE, T. : 1457.
ABELES, F.B. : 1,2.
ABON, C. : 258.
ABRAHAMS, S.J. : 1367.
ABRAMOWITZ, J. : 3.
~ :
ACKERMAN, GA : 4.
ADAMS, Jr. W.R. : 5.
ADAMS, PA : 6.
AHERN, T.J. : 7.
AHFORS, C.E. : 163.
AHLUWALIA, S. : 519, 519a.
AHMED, S. : 7a.
AHUJA, B.S. : 8.
AHUJA, M.R. : 9.
AKlYAMA, M : 1205.
AKSENOVA, V.A : 1126.
AKULOVA, E.A. : 919.
AL-AZZAWI, M.J. : 10,513.
ALBALA, A. : 957.
ALBUZIO, A. : Il.
ALCAREZ, C. : 186.
ALESHIN, E.P. : 887.
ALEXANDER, M.B. : 313.
ALEXANDER, N.M. : 12, 702.
ALEXANDRESCU, V. : 13, 14, 15,506.
ALEXEEVA, V.J. : 1298.
ALFSEN, A. : 16.
ALGHISI, P. : 17.
ALI, A. : 18.
ALI, M.H. : 19.
ALIBERT, E. : 20.
ALLAN, G.G. : 7.
ALLARD, R.W. : 234, 523, 832, 833.
ALLDRIDGE, NA : 468.
ALMGARD, G. : 21, 22, 23, 24, 25.
AMIN, J.V. : 1232.
ANDERSON, J.O. : 1371.
ANDERSON, L.C : 26.
ANDERSON, W.A. : 27, 28, 175, 227, 316.
256 PEROXIDASES 1970/1980
ANDREEVA, VA : 29.
ANSTINE. W. : 30.
ANTAKLY, T.W. : 31,970.
ANTONINI, E. : 16, \032. 1033. 1034.
ANTOSZEWSKI, R. : 267. 268,440, 1134
AR, N.P. : 636.
ARAISO, T. : 31a, 32, 33. 345, 1460.
ARAKAWA, H. : 34.
ARCENEAUX, D. : 273.
ARCHER, J.M. : 1117.
ARMSTRONG, A : 937.
ARMSTRONG, D. : 35, 1291.
ARNISSON, P.G. : 36, 37, 38, 39, 40.
ARUTYUNYAN, AM. : 810.
ARYA, H.C. : 1060, 1060a, 1060b, lO73a, lO73b.
ASADA, K. : 41.
ASADA, Y. : 967.
ASAKUA, T. : 1311.
ASTHANA, J.S. : 1254.
ATACK, AV. : 1154, 1155.
ATAULLAKHANOV, F.l. : 379.
ATSUMI, S. : 42.
AUDERSET, G. : 282, 479.
AUGUSTO, O. : 228.
AULIKKI, M.S. : 43.
AUSSEL, C. : 326.
AUSTIN, J.H. : 1291.
AUNE, T.M. : 44, 1323, 1324.
AVER'YANOV, AA : 45.
AVISSE, C. : 1397.
AVRAMEAS, S. ; 46, 160, 1057, 1337.
AWASTHI, Y.G. : 47.
AZEN, EA : 48.
BABBLE, G.R. : 1213.
BABOSZEBENYI, E. : 1369.
BACON, D.R. : 666.
BADEN, D.G. : 49, 50.
BAG, A. : 912
BAILLAUD, L. : 140.
BAINTON, D.F. : 145.
BAJAJ, S. : 51, 52.
BAJAJ, Y.P.S. ; 51, 52.
BAKARDJIEVA, N.T. ; 52a, 54, 54a, 54b, 54c, 55, 56, 57, 58, 58a, 59, 308,460,461.
BAKER, B. : 524.
257 AUTHORINDEX
BAKER, B.L. : 524
BALA, S. : 1299.
BALABAEV, N.K. : 379.
BALASIMHA, D. : 60, 61, 62, 63, 64, 65, 66, 1070, 1071, 1072.
BALAZS, E. : 419.
BALDWIN, DA : 6.
BALLAL, S. K. : 1191.
BANDURSKI, R.S. : 237.
BANERJEE, R.K. : 204.
BANERJI, A. : 67
BANERJI, D. : 1143
BANGERTH, F. : Ina.
BANKSTON, P.W. : 1042
BAR-AKIVA, A. : 1140.
BARBARA, D.J. : 68, 1451.
BARBAS, H. : 867.
BARBOTIN, J.N. : 69.
BARDSLEY, W.G. : 70, 217, 1209.
BARKER, C.W. : 73.
BARKER, W.G. : 985.
BARNA, J. : 71.
BARNETT, N.M. : 72,261.
BARTLlNG, Q.J. : 73.
BARZ, W. : 74,97, 573.
BASHOUR, N. : 384, 390.
BASSIRI, A. : 75, 75a.
BASTIN, M. : 76, 77, 78, 79.
BATCHELOR, A.O. : 246.
BATES, D.C. : 80, 198.
BATES, L.S. : 980.
BATRA, G.K. : 81.
BAULT, A. : 82.
BAUMANN, G. : 565.
BAUN, L.c. : 936.
BAVER, N. : 147.
BAXTER, R. : 279.
BAYSE, G.S. : 83, 84, 85, 907, 908, 909.
BAZIN, M. : 646.
BEAL, E.A. : 1049.
BEARD, M.E. : 957.
BECHARA, EJ.H. : 86, 228, 960, 1410.
BECK, G.E. : 515a, 784.
BECKMAN, C.H. : 910.
BEDNAR, T.W. : 87, 88.
BEEVERS, H. : 1477.
BELDING, M.E. : 89.
BEMILLER, J.N. : 90.
BENADA, J. : 91.
258 PEROXIDASES 1970/1980
BENDALL, D.S. : 1076.
BENEDICT, W.G. : 92, 93.
BENES, K. : 94, 502.
BENITO, C : 95.
BENIWAL, S.P.S. : 1341.
BERA, A. K. : 206.
BEREZIN, I.W. : 96, 730, 731, 732, 1358, 1359, 1361, 1362, 1466.
BERGH, B.O. : 1333, 1334, 1335.
BERLIN, J. : 97.
BERNHARD, W. : 31.
BERTAUX, B. : 333.
BERVILLE, A. : 434.
BESFORD, R.T. : 98.
BESTER, A.I.J. : 1385, 1386, 1387.
BEUTLER, E. : 47, 1167.
BEWLEY, J.L. : 1274.
BHARGAVA, K.S. : 99.
BHARTI, S. : 99a.
BHATIA, CR. : 882, 883.
BHATTACHARYA, N.C : 100, 101,323,930,931,932.
BHATTARCHARYA, S. : 100, 102, 103,714,911.
BIDLACK, W.R. : 104.
BIELER, L.Z. : 183.
BIELSKI, B.H.J. : 105, 106, 107.
BIEMPICA, L. : 957.
BILLETT, E.E. : 1238.
BIRECKA, H.: 108, 109, 110, 111,112,113,114,115,116,188.
BIRKNER, M. : 482.
BISWAL, V.C : n 93.
BISWAS, B.B. : 1080a.
BJORKSTEN, F. : 117, 118.
BLAAS, J. : 156, 157.
BLAICH, R. : 119.
BLANC, B. : 1037.
BLIGNY-FORTUNE, D. : 120, 569, 570.
BLOOM, G.D. : 121, 185.
BLOOMBERG, R. : 527, 1355.
BLOOMGARDEN, D. : 1422.
BLUM, H. : 1104.
BLUME, D.E. : 122.
BLUME, K.G. : 164, 1167.
BLUTHNER, W.D. : 578.
BLYUMENFELD, L.A. : 810.
BOGDAN, S. : 123.
BOISARD, J. : 1025.
BOLL, W.G. : 36, 37, 38, 39, 40.
BOLLER, Th. : 124.
BONNER, W.D. : 1103, 1104.
259 AUTHOR INDEX
BONFANTE-FASOLO, P. : 124a.
BONISOLLl, F. : 125.
BONZON, M. : 479.
BOORSMA, D.M. : 126.
BOOP, M. : 51,52, 126a, S03, S04, S05, S06, 807.
BORCHERT, R. : 127, 129, J30.
BORODENKO, L.1. : 10/3.
BORYS, M.W. : 1294.
BOS, A. : 131.
BOSMAN, ET. : 132.
BOTTGER, M. : [33.
BOUCHET, M. : 133, 134, 135, 135a, 136,338,435,436,437,438,439,452674,851,852.
BOUDET, A.M. : 20.
BOUILLENNE, C. : 137.
BOVERIS, A. : 138, 1103.
BOWLING, A.c. : 139.
BOXUS, P. : 1063.
BOYER, N. : 140, 141, 142, 143, 144.
BOZALIK, S.J. : 1388.
BOZDECH, M.J. : 145.
BRABER, J.M. : 146.
BRAD, 1. : 146a, 254, 914, 1043, J223.
BRADER, J.M. : 146.
BRATTON, B.O. : 147, 148.
BRAVINDER-BREE, S. : 1262.
BREDEMEIJER, G.M.M. : 149, [50, 151, 152, 153, 154, 155, 156, 157.
BREDEROO, P. : 989.
BRENNAN, T. : 158.
BRETON-GORIUS, J. : 159, 825.
BRETTON, R. : 160.
BREWBAKER, J.L. : 160a, 1010.
BRIBER, K.A. : 108.
BRIGHT, J.E. : 1321.
BRIGNAC, Jr. P.J. : 273.
BRINKMANN, F.G. : 161.
BRITTAIN, M.G. : 162.
BROCK-LE-HURST, E. : 362.
BRODERSEN, R. : 163.
BRODRICK, H.T. : 1389, 1390, 1391. !
BRONNIKOVA, T.V. : 379.
BROOKS, J.L. : 696, 697.
BROSS, R.J. : 164, 1167
BROUET, A. : 123.
BROYKO, L.K. : 1358.
BROWN, A.H.D. : 73, 165.
BROWN, L.F. : 1443.
BROWN, R.H. : 166
BROWNING, A. : 1062.
260 PEROXIDASES 1970/1980
BRULFERT, J. : 167.
BRUNNER, H. : 168.
BRUNORI, M. : 1032, /033, 1123, 1441.
BRYANT, S.D. : 169.
BRYGIER, J. : 170.
BRZOZOWSKA-HANOWER, J. : 171.
BUDILOVA, E.V. : ln.
BUDU, C.E. : 838.
BUFLER, G. : Ina.
BUGBEE, W.M. : 173.
BUIS, R. : 174, 1031.
BU KOVAK, M.J. : 1046, 1444.
BUNT, A.H. : 194.
BURG, S. : 653.
BURKE, R.E. : 522.
BURLESTON, B. : 1445.
BURNETT, C. : 27, 175.
BURR, B. : 939.
BURUIANA, L.M. : 176.
BUSINELLI, M. : 1307.
BUTTON, J. : 177.
CABANNE, F.R. : 178.
CABRILLAT, H. : 179.
CACCO, G. : Il, 1251.
CACHITA-COSMA, D. : 180, 181.
CAIRNS, E. : 182.
CAIRNS, W.L. : 182, 1381a.
CALVAN, M. : 1273.
CALVO, R. : 842.
CAMERON, P.V. : 243.
CAMMER, W. : 183.
CANNON, A.M. : 184.
CANNON, M.S. : 184.
CAPONETTI, J.D. : 905.
CAPRON, T.M. : 1427a.
CARDENAS, F. : 764.
CARLSON, J.A. : 632.
CARLSON, P.S. : 75, 75a.
CARLSOO, B. : 121, 185.
CARPENA, O. : 186.
CARSON, KA : 867.
CARTER, D.P. : 187.
CARUBELLI, R. : 1350.
AUTHORINDEX 261
CARUSO, J.L. : 19,
CASADEI DE BAPTISTA, R. : 86, 228.
CASHORE, W.J. : 163.
CASTILLO, F. : 187a.
CATALFAMO, J. L. : 108, 109, 110, 1Il, 188.
CATEDRAL, F. : 189, 1181.
CATESSON, A.M. : 190, 190a, 191, 192, 193,265,266.
CAUBERGS, R. : 292.
CAVALIERI, A.J. : 461a.
CAVALIERI, E.L. : 1119.
CAVATORTA, P. : 378.
CECCHINI, J.P. : 871, \028.
CECH, F.e. : 591.
CERNOHORSKA, J. : 352.
CEULEMANS, E. : 452.
CHABIN, A : 646.
CHADWICK, AV. : 255
CHAMPAULT, A. : 646.
CHAN, H.S. : 1427a.
CHAN, K.Y. : 194.
CHAN, P.e. : 106.
CHANCE, B. : 195.
CHANDRA, G.R. : 196, 197.
CHANG, e.K. : 32.
CHANG, J.Y. : 197a.
CHANT, S.R. : 80, 198.
CHAPELLE, B. : 141.
CHAPPET, A : 199, 200, 201, 202, 203, 335, 484.
CHASKES, M.J. : 112.
CHATTERJEE, D.K. : 204.
CHATTOPADHYAY, N.e. : 206.
CHATTOPADHYAY, S. : 73,205.
CHAVAN, P.D. : 221.
CHAUDHARY, S.S. : 723.
CHAUHAN, J.S. : 207.
CHAVIN, W. : 3.
CHEIGNON, M. : 208.
CHEN, S.L. : 209.
CHERIAN, R. : 809.
CHERNOFF, S. : J080.
CHERRY, J.P. : 210, 211.
CHERSI, A. : 1187.
CHERTAL, K. : 809.
CHETAL, S. : 212.
CHI, E.Y. : 537.
CHIANCONE. E. : 16.
CHIBBAR, R.N. : 213.214,215,933.
CHIGRIN, V.V. : 216.
262 PEROXIDASES 1970/1980
CHILDS, R.E. : 217, 1209.
CHIN, e.Z. : 218.
CHIPKO, B.R. : 246.
CHIRKOVA, T.V. : 219.
CHMIELNICKA, J. : 220.
CHOUDHARY, S.S. : 221.
CHOUREY, P.S. : 222.
CHOY, Y.M. : 223, 1479.
CHRISTIE, K.N. : 224, 225.
CHU, M. : 225a.
CHUNG, J. : 226.
CHUNG, K. : 761.
CHUNG, A. : 227.
CHYLINSKA, K.M. : 684.
CILENTO, G. : 86, 228, 350 860 960 1409, 1410, 1411, 1486.
CIOPRAGA, J. : 229.
CLAIRBONE, A. : 230, 231, 232.
CLAIRE, A.: 140.
CLAPHAM, D. : 22, 23.
CLARK, H.D. : 197.
CLARK, MA : 4.
CLARKE, J. : 233.
CLARKSON, R.B. : 591.
CLEGG, M.T. : 234.
CLELAND, R. : 424, 425.
CLEMENTI, F. : 235.
CLOCHARD, A. : 1397.
CLYNE, D.H. : 236.
COHEN, e. : 1422.
COHEN, J.D. : 237.
COHEN, Y. : 238.
COHEN: ZA : 593, 1269, 1270.
COLD, M.H. : 703.
COLILLA, W. : 90.
COLLIER, G.S. : 6.
COLLIER, H.B. : 239.
COLLNGS, J.R. : 240.
COLLINS, N. : 166.
COLLINS, T. : 1422
COLOTELO, N. : 1182.
COMBATT1, N.e. : 222
COME, D. : 1320.
COMSTOCK, DA : 106.
CONKLIN, M.E. : 241, 1238a.
CONSTABEL, F. : 242.
CONTIN, G.G. : 1400.
COOKE, e.T. : 243.
COOMBES, AJ. : 244.
AUTHOR INDEX 263
COPES, D.L. : 245.
CORBETT, M.D. : 49, 50, 246.
CORIN, R.E. : 247.
COSMIN, O. : 914.
COTRAN, R.S. : 248, Il 16.
COTTON, M.L. : 249, 250.
COUDERC, H. : 342.
COULOMB, P. : 251, 1347.
COULSON, A.F.M. : 252.
COUPE, M. : 253.
COURDUROUX, J.c. : 447.
COVOR, A. : 254.
COX, C.D. : 247.
CRAIG, M.E: : 1420.
CRAKER, L.E.: 2, 255.
CRAMER-KNIJNENBURG, G. : 132.
CRITCHLOW, J.E. : 256, 257, 257a.
CRONENBERGER, L. : 258.
CROWOEN, R.K. : 139.
CSERESNYES, Z. : 506.
CUNNINGHAM, B.A. : 259, 630, 733, 760, 761, 1138.
CURTIS, C.R. : 260, 261, 262, 263, SOI.
CZANINSKI, Y. : 192, 193,264,265,266,466.
CZAPSKI, K. : 267, 268.
CZARNECKA, E. : 1441.
DABROWSKA, T. : 1055.
DAEMS, W.T. : 269.
DA GRACA, J.U. : 269a.
DALY, J.M. : 189, 270,271, 271a, 271b, 1180, 1181.
DANNER, D.J. : 272, 273, 909.
DARBYSHlRE, B. : 274, 275, 276.
DARIMONT, E. : 277,278,279,280,281,282,283,434,437,577, 1015, 1016, 1017.
DASGUPTA, P. : 102,714.
DASHEK, W.V. : 284.
DASS, H.C. : 285.
DATTA, A.G. : 204.
DAUPHIN, B. : 646.
DAUSSANT, J. : 286, 287, 1124a, 1234.
D'AUZAC, J. : 253.
DAVIDSON, B. : 288, 937.
DAVIES, D.D. : 1137.
DAVIES, D.M. : 289.
DAVIES, M.E. : 290.
DAVIS, C. : 958.
264
PEROXIDASES 1970/1980
DAVIS, L. : 973.
DAVYDOV, R.M. : 810.
DAVYDOVA, MA : 609.
DEAL, CL. . 384, 385.
D E C H A T E L E ~ R. :8TI.
DEDECUE, CJ. : 130.
DEEN, J.L.W. : 98.
DEGN, H. : 291, 975, 975a.
DE GREEF, J.A. : 292.
DEGROOT, Ll. : 922.
DEIMANN, W. : 293.
DEJAEGERE, R. : 1139.
DE JONG, D.W. : 294, 295.
DEKOCK, P.c. : 296, 297.
DELAIGUE, M. : 646.
DELFIACCO, M. : 1114.
DELINCEE, H. : 298 299 300, 301, 302, 303, 304, 305, 1068a, 1326.
DELLACORTE, L. : 1188.
DELRIO, I.A. : 306, 307.
DEMIREVSKA-KEPOVA, K. : 55, 56, 57,308.
DEMOREST, D.M. : 309, 1264, 1265.
DEMORROW, J.M. : 547, 548.
DENCHEVA, A.V. : 310, 311, 682.
DENDSAY, J.P.S. : 312.
DENNA, D.W. : 313.
DENNY, P. : 553.
DE OLMOS, J.S. : 314.
DEPREST, B. : 1118.
DE ROPP, J.S. : 724a.
DE RYCKER, J. : 315, 520.
DESARLO, F. : 1188.
DESCHAMPS-MUDRY, M. : 200.
DE SOMBRE, E.R. : 316, 317, 780, 781, 782.
DESSER, R.K. : 318.
DEVAY, M. : 699.
DEVI, G. : 319.
DEVILLERS, E.A. : 877.
DEWOLF, M. : 320.
DEZSI, L. : 321, 322.
DHALIWAL, G. : 323.
DHAWAN, A.K. : 324.
DICKS, J. W. : 325.
DIETRICK, W. : 320.
DIJKMANS, H. : 77.
DIMITRIJEVIC, L. : 326.
DINELLO, R.K. : 327.
DIXON, L. : 35.
DJAVADI-OHANIANCE, L. : 328.
j.-
i:
265 AUTHORINDEX
DOELLGAST, G.l. : 1318.
DOLARA, P. : 1188.
DOLMAN, D. : 329.
DOLPHIN, D. : 327.
DOMBROVSKlI, VA : 732.
DONNELLAN, B. : 971.
DO QUY HAl, : 330, 508.
DORRIS, M.L. : 1080.
DOUBEK, D.L. : 505.
DOUGHERTY, H.W. : 710.
DOUMENJOU, N. : 331.
DOUSCHKOVA, P.1. : 310.
DOUZOU, P. : 331a, 1338.
DOYLE, M.P. : 332.
DRAWERT, F. : 303, 304.
DRESLER, S. : 1263.
DREYFUS, B. : 825.
DROBYSHEVA, N.1. : 1011.
DROUET, A. : 1303.
DUBERTRET, L. : 333.
DUBIN, l. : 1415.
DUBOIS, J. : 747, 748.
DUBOUCHET, J. : 201, 202, 203, 334, 335, 336, 423a, 483, 484, 1058.
DUBUCQ, M. : 337, 338, 440,441, 442, 674.
DUDEN, R. : 339.
DUFFUS, C.M. : 340.
DUFFY, G. : 341.
DUFFY, M.J. : 341.
DUMITRESCU, M. : 342.
DUMITRU, I.F. : 605.
DUNFORD, H.B. : 31a, 32, 225a, 249, 250, 256, 257, 257a, 329, 343, 344, 345, 346,
347, 347a, 531,563,624,625,628,629,633,920, 920a, 928, 1069, 1120,
1121, 1122, 1268, 1275, 1276.
DUNLAP, T.W. : 1420.
DUNLEAVY, J.M. : 348, 1364, 1365. 1366.
DURAN, N. : 86, 228, 349, 350, 860, 960, 1409, 1410, 1411, 1486.
DURAND, B. : 646, 776.
DURAND, R. : 646.
DURZAN, D.J. : 1073.
DUTTA, S. : 67.
DUVAL, J.c.c. : 351.
DVORAK, M. : 352.
DYM, M. : 1014.
DZlEWANOWSKA, K. : 353.
266 PEROXIDASES 1970/1980
EARL, J.W. : 354.
EDELSTEIN, L.M. : 971, 997.
EDREVA, A.M. : 355, 1127.
EGAN, R.W. : 710.
EGUCHI, H. : 652a.
EHRENBERG, A. : 817.
ELKINAWY, M. : 356.
ELLIOTT, M.e. : 1429.
EL-METHANY, A. : 356a.
ELSTNER, E.F. : 357,489.
EMANOVILOV, E. : 57.
ENDERS, N.T. : 164.
ENOO, T. : 358, 984, 1474.
ENDRESS, A.G. : 359.
ENSINK, F. T.E. : 1373.
EPSTEIN, D. : 997.
EPSTEIN, E. : 360.
EPSTEIN, N. : 361, 1162.
ERECINSKA, M. : 362.
ERICKSON, S.S. : 284.
ERMAN, J.E. : 252, 363.
ERNEST, L.e. : 364.
ESEN, A. : 365.
ESQUERRE-TUGAYE, M.T. : 850.
ESSNER, E. : 366, 367.
ESTERBAUER, H. : 368, 369, 482.
ESTERHUIZEN, E.W. : 1390, 1391.
EURELL, T.E. : 184.
EVANS, J.J. : 370, 371.
EVANS, M.L. : 372, 373.
EVANS, W.H. : 318.
EVANS, R.e. : 425c.
EVETT, M. : 1122
FACCIOLl, G. : 374.
FAHIMI, H.D. : 293, 375, 376, 377, 558, 559, 1116, 1402.
FALCIONI, G. : 1123.
FAUONI, A. : 228, 349, 860, 1409.
FALLOT, J. : 427.
FARKAS, G.L. : 322, 729a.
FARKAS, J. : 1369.
FARRIMOND, J.A. : 1429.
FATRAI, Z. : 1220.
FAVILLA, R. : 378.
FEDAK, G. : 378a.
AUTHOR INDEX
FEDKINA, V.R. : 379.
FEILLET, P. : 619, 686, 688.
FEINBERG, J.H. : 188.
FEINGOLD, M. : 380.
FEJER, O. : 699.
FELBERG, N.T. : 381.
FELD, R.D. : 1443.
FELDER, M.R. : 382.
FEL'DMAN, D.P. : 96.
FENIL[, D.: 1488.
FERET, P.P. : 383, 848.
FERRARI, G. : 1251.
FERRI, M.V. : 383a, 494.
FEUCHT, W. : 1166.
FEUNG, C.S. : 522.
FIBIGER, H. : 1266.
FIELDES, MA : 384, 385, 386, 387, 388, 389, 390, 1356, 1357.
FIELDING, J.L. : 391,392, 513.
FINK, B. : 393.
FIORETTI, E. : 1123.
FITES, R.C. : 1329, 1330.
FLECHTER, RA : 18, 620, 621.
FLOYD, RA : 1086.
FLCKIGER, W. : 394, 395.
FLCKIGER-KELLER, H. : 395.
FLURKEY, W.H. : 396, 397.
FOBES, J.F. : 1105, 1106, 1107.
FONG, K.L. : 783.
FONTAINIERE, B. : 179.
FORLANI, L. : 1034.
FORRENCE, L.E. : 2.
FOSKET, D.E. : 1336.
FOSSE, M. : 333.
FOWLER, J.L. : 398, 894.
FRANCALANCI, R. : J 188.
FRENKEL, C. : 158, 218, 399, 400, 402, 404, 499.
FRETZ, TA : 712, 713.
FRETZDORFF, B. : 405.
FREY, G. : 573.
FRIC, F. : 406, 407, 408, 409.
FRICKER, A. : 339, 995.
FRIDOVICH, I. : 230, 231, 232, 532, 881.
FRIEDEN, E. : 594.
FRIEDHOFF, J.M. : 530.
FRIEND, J. : 410.
FRlES, D. : 411, 412, 413, 438, 439, 443.
FRY, S.c. : 414,415.
FRYDMAN, B. : 416.
FRYSMAN, R.B. : 416.
267
,
,.
268 PEROXIDASES 1970/1980
FUCHS, W.H. : 409, 859.
FUJITA. H. : 417, 663.
FUJITA, S. : 418.
FU KAt K. : 972.
FUKUNAGA. T. : 972.
FURAI, K. : 972.
FUSHIKI, H. : 926.
GABORJANYI, R. : 419.
GALE, M.D. : 420.
GALLATI, H. : 421, 421a.
GALLIANI, G. : 422.
GALLIARD, T. : 423.
GALLOIS, T. : 423a, 484.
GALSTON, A.W. : 5, 113, 116, 665, 753, 754, 955, 956.
GAMLIN, P. : 1090.
GANCEVA, K. : 787.
GARAY, R.V. : 782.
GARBER, E.D. : 1081.
GARCIA-RODRIGUEZ, M.J. : 120.
GARDINER, M.G. : 424, 425.
GARG, O.P. : 1204.
GARRAWAY, M.O. : Ill, 114, 425a, 425b, 425c.
GARRETT, J.R. : 426.
GARR1S0N, L.B. : 666, 667.
GAS, C. : 427.
GASPAR, Th. : 133, 134, 135, 135a, 136, 137, 141, 142, 143, 144, 180, 181, 280,
281,282,283,338413,428,429,430,431,432,433,434, 435, 436, 437,
438, 439, 440, 441, 442, 443, 444, 445, 446, 447, 448, 449, 450, 451,
452, 577, 674, 749, 938, 1015, 1016, 1017, 1063, 1133, 1320, 1327, 1328,
1374, 1375.
GASYNA, Z. : 453.
GAUTHIER, M.F. : 687.
GEBICKI, J.M. : 107.
GEELEN, J.L.M. : 1395.
GEIGER, J.P. : 454, 455.
GELINAS, DA : 456.
GEMANT, A. : 457, 457a,
GENTILE, I.A. : 458.
GENTINETTA, E. : 1248, 1249.
GEORGE, W.L.Jr. : 874.
GEORGESCU, C.M. : 459.
GEORGIEV, G.H. : 58,460,461.
GEORGIEV, G.K. : 461.
GETTYS, K.L. : 461a.
AUTHORINDEX 269
GEWITZ, H.S. : 462.
GEYER, G. : 695.
GHAZY, AM. : 650, 651.
GHOSH, B. : 1185.
GHOSH, J.K. : 462a.
GIACOMETTI, G. : 1033.
GIBSON, D.D. : 783.
GIBSON, D.M. : 463,464, 767.
GIBSON, Q.H. : 950.
GICHNER, T. : 1302.
GIEBEL, J. : 465, 1439.
GILES, A.B. : 1238.
GIRAUD, G. : 466.
GLASIUS, E. : 1373.
GOFF, c.w. : 467, 809
GOLDSTEIN, J. : 112.
GOMEZ, M. : 306, 307.
GONATAS, NA : 526.
GONATAS, T.O. : 526.
GONZALEZ-ALONZO, L.M. : 843.
GOPINATHAN, K.P. : 319.
GORDON, AR. : 468.
GORDON, G.J. : 549.
GORDON, J.c. : 469, 1447, 1453.
GORDON, W.R. : 470.
GOREN, R. : 442.
GORENFLOT, R. : 342.
GORIN, N. : 125, 471.
GORZ, H.J. : 618.
GOTLIEB, A : 1422.
GOUJON, M. : 454, 455.
GOVE, J.P. : 472, 473.
GOWER, E.C. : 867.
GREEN, R.C. : 474.
GREGORY, L.E. : 196, 197.
GREIMEL, A. : 475, 476, 477, 478.
GREPPIN, H. : 135a, 187a, 282, 444, 445, 479, 658,659,660,661,749. 1015, 1016,
1017, 1018, 1019, 1020, 1021, 1022, 1023,1024, 1025, 1026.
GRIFFIN, B.W. : 480, 481.
GRILL, D. : 369, 482.
GRISEBACH, : 507.
GRISON, R. : 483, 484, 485, 1058.
GROB, K. : 486.
GROOME, N.P. : 487.
GROSS, G.G. : 487a, 488, 488a, 489.
GROSSER, C. : 1253.
GROVER, Y.P. : 490.
GRZELINSKA, A : 491.
PEROXIDASES 1970/1980 270
GUARNA, A. : 1188.
GUHAMUKHERJEE, S. : 613, 1194, 1195, 1196, 1197, 1198.
GUIBERT, B. : 46.
GUPTA, B.D. : 913.
GUPTA, V.K. : 9, 492, lOCH, 1340.
GURUMURTl, K. : 213,214, 215, 493, 933.
GURUPRASAD, K.N. : 723.
GUST1N, M.K. : 962.
GUZMAN, C.A. : 383a, 494, 495, 1342.
HAARD, N.F. : 402, 496, 497, 498, 499, 500, 923, 1074.
HABECK, H. : 50\.
HABER, A. : 106.
HADACOVA, V. : 502.
HADDON, L. : 503.
HADLER, W.A. : 1216.
HAGER, A. : 504.
HAGER, L.P. : 505, 563a, 1325.
HAG1MA, 1. : 13, 14, 506.
HAG1WARA, T. : 604a.
HAHLBROCK, K. : 507.
HAl, D.Q. : 330, 508.
HA1SMAN, D.R. : 509.
HA1SS1G, B.E. : 510.
HALDMANN, M. : 511.
HALL, A. : 296.
HALL, H.G. : 512.
HALL, J.L. : 10,391,392,513, 5J4, 515, 593.
HALL, T.C. : 515a, 784.
HALLlWELL, B. : 315,516,517,518,519, 519a, 520.
HALPER1N, W. : 521, 878, 879.
HAM, E.A. : 710.
HAMADA, G. : 971.
HAMA KER, J.M. : 1245.
HAMBR/CK, J.L. : 523.
HAMERS, M.N. : 1433.
HAM/LL, D.E. : 1239.
HAM/LTON, R.H. : 522.
HANCHEY, P. : 524.
HANCOCK, J.f. : 461a.
HANOWER, P. : 171, 524.
HARGIS, J.H. : 505.
HARKIN, J.M. : 525.
HARPER, c.G. : 526
HARRIS, A.B. : 1351.
271 AUTHOR INDEX
HARRIS, J.W. : 1191.
HART, G.E. : 1164.
HART, MA : 527.
HARTE, C. : 1179.
HARTENSTEIN, R. : 528, 529.
HARTMANN, C. : 123, 1303.
HASCHKE, R.H. : 194, 530. !.
HASEGAWA, Y. : 160a.
HASINOFF, B.B. : 531.
HASKINS, FA : 628.
HASSAN, H.M. : 532.
HAUN, M. : 228.
HAWKINS, RA : 1027.
HAYASHI, T. : 42.
HAYASHI, Y. : 533, 534, 535, 1460.
HAYWARD, D.M. : 284.
HEGARTY, E. : 867.
HEIDEMA, ET. : 471.
HEINTZE, K. : 339.
HEIPERTZ, R. : 1039.
HELLIN, E. : 186.
HEMPHILL, D.Jr. : 1467, 1468
HENDERSON, J.H.M. : 470, 536.
HENDERSON, W.R. : 537, 538, 539, 540, 634.
. HENDRIKS, T. : 541.
HENRIKSON, A. : 1003.
HENRY, E. W. : 147, 148, 543, 544, 545 546, 547, 548, 549, 550, 551, 552, 553, 554.
HENRY, Y. : 555.
HEPLER, P.K. : 556, 1336.
HERSZKOWICZ. 1. : 495.
HERZOG, V. : 377, 557, 558, 559, 560 561, 562.
HESS, C.E. : 404.
HEUPEL, A.L. : 357.
HEWETT, D. : 1368.
HEWSON, W.D. : 346, 347, 563, 563a.
HEYNE, E.G. : 259.
HIDAKA, H. : 922.
HIGUCHI, T. : 564, 926.
HILDERSON, H.J. : 320.
HILGENBERG, W. : 565.
HILL, J.H. : 1366a.
HILL, J.M. : 566
HIMMELHOCH, S.R. : 318.
HIRAI, K. : 567.
HIRANO, H. : 1471.
HIROMI, K. : 900.
HIRSCH, A.M. : 120, 568, 569, 570.
HISLOP, E.C. : 571.
272 PEROXIDASES 1970/1980
HOBNER, G. : 1253.
HOBSON, G.E. : 572.
HOEK. F.J. : 1143a.
HOESEL, W. : 573.
HOESS, R.H. : 574.
HOFFEREK, K. : 575, 576.
HOFFMANN, M.E. : 729b, 860.
HOFFSTEIN, S. : 1422.
HOFINGER, M. : 281, 577.
HOHLER,B. : 578.
HONlG, D.H. : 1068.
HORN BROOK, K.R. : 783.
HORSMAN, D.O.: 579, 580, 1427a.
HORVATH, M.M. : 581.
HOSHINO, Y. : 1184.
HOWELL, R.K. : 262, 263.
HOYLE, M.C. : 472, 473, 582 583, 584, 585, 586, 587.
HRADILIK, J. : 588.
HRYCAY, E.G. : 589, 590.
HUANG, F.H. : 591.
HUAULT, C. : 592.
HUBBARD, A.L. : 593.
HUBER, CT. : 594.
HUBERMAN, M. : 442.
HUBNER, G. : 1253.
HUDEK, J. : 1277.
HUISINGH, D. : 597.
HUMES, J.L. : 710.
HURDUC, N. : 254.
HUSSEY, R.S. : 595, 596, 597.
IDA, 5. : 598, 599, 903.
IIZUKA, T.c. : 678.
IMAIZUMI, K. : 1206.
IMASEKl, H. : 600, 1190.
IMBERT, M.P. : 601, 602, 603.
INKSON, R.H.E. : 296.
INNOCNETI, A.M. : 604.
INOUYE, J. : 604a.
INSLER, V. : 380.
IN1JBUSHI, T. : 899.
IORDACHESCU, D. : 605.
15H11, H. : 1205.
15H11, T. : 716.
AUTHORINDEX
ISHIMARU, A. : 606.
ISHIMURA, Y. : 678.
IVANOVA, MA : 172.
IVANOVA, N.N.: 607,6081011,1012.
IVANOVA, T.M. : 609,610.
IWASA, S. : 652a.
IWASAKl, K. ; 716.
IYANAGI, T. : 1156.
JACOBS, A.A. : 611.
JACOBS, M. : 180, 181, 938.
JACOBSEN, J.V. : 30.
JAEGER-WUNDERER, M. : 612.
JAGANNATH, D.R. ; 883.
JAIN, A. : 1254.
JAIN, S.K. : 1225, 1226.
JAIN, S.M. : 613.
JAISMAL, V. : 613a, 1115.
JAMALE, B.B. : 614.
JAMES, G. T.: 1291.
JANKAY, P. : 615.
JANKELEVICH, B.B. : 947.
JANSE, C. ; 489.
JANSSEN, M.G.H. : 616.
JANUSKA, M. : 318.
JASANI, B. ; 617
JAYASA, N.K. ; 636.
JAYNES, TA : 618.
JEANJEAN, M.F. ; 619.
JELLINCK, P.H. : 620,621,622,668, 794, 795.
JEN, J.1. : 396, 397, 1326a.
JENNINGS, A.C. : 623.
JENSEN, T.E. : 550, 554.
JERINA, D.M. : 271b.
JEVNlKAR, J.J. ; 744.
JOASSIN, L. : 135.
JOB, C. : 851.
JOB, D. : 200, 225a, 624, 625, 626, 627, 628, 629, 1059. 1101.
JOHAM, H.E. : 895.
JOHN, K.V. ; 940.
JOHNSON, L.B. : 630, 631.
JOHNSON, MA : 632.
JONARD, R. : 1043a.
JONAS, D.E. : 1220.
273
i
274 PEROXIDASES 1970/1980
JONES, D.G. : 243.
JONES, L.R. : 1348.
JONES, P. : 289, 626, 633.
JONG, E.C. : 538, 634, 635.
JORDAN, W. : 551.
JOSEFSSON, J.O. : 779.
JOSEPH, K.V. : 636.
JOSH1, G.c. : 1299.
JOSH1, G.V. : 614.
JOSH1, M.G. : 1075.
JOSH1, M.M. : 1299.
JOSH1, R.D. : 99.
JOUBERT, AJ. : 637.
JUDEL, G.K. : 638, 639.
JULAVEANU, A : 13.
JULIANO, B.O. : 936, 986.
JUNG, GA : 700.
JUNGHANS, P. : 1253.
JUNIPER, B.E. : 1117a.
JUO, P.S. : 640.
KACHAR, B. : 1411
KACPERSKA-PALACZ, A : 641.
KAOOUM, AM. : 1138.
KAHL, G. : 642.
KAHLEM, G. : 643, 644, 645, 646.
KA LINER, M. : 539.
KALYANARAMAN, V.S. : 647,648.
KAMBOJ, R.K. : 649.
KAMEL, M. Y. : 650, 651.
KAMINSKI, C. : 652.
KAMISAKA, S. : 1142.
KANAZAWA, K. : 652a.
KANG, B.G. : 653.
KANG, C.H. : 941.
KANG, Y.H. : 28,316.
KANG, Y.J. : 654.
KAOSIRI, T. : 655.
KAPLAN, R. : 1422.
KAPLOW, L.S. : 656.
KAR, M. : 657.
KARADGE, BA : 221.
KARATAGLIS, S. : 1304.
KAREGE, F. : 658, 659, 660, 661, 1026.
AUTHOR INDEX 275
KARNOVSKY, M.J. : 1014, 1296. 1297.
KATAOKA. K. : 662,663.
KATO, M. : 664.
KATO, Y. : 1309.
KATOH. T. : 1205.
KATOMSKI, PA : 1119.
KAUR, N.P. : 101,930,931.
KAUR, S.P. : 816a.
KAUR-SAWHNEY, R. : 665, 754.
KAVANAGH, J. : 70.
KAWAI, N. : 1471.
KAWARDA, A. : 1300.
KAY, E. : 1208, 1293.
KEEN, N.T. : 996.
KEENAN, EJ. : 666, 667.
KEEPING. H.S. : 668.
KEFELI, V. : 669.
KELLER. T. : 670, 671,672.
KELLY, G.J. : 673.
KEMP, E.D. : 667,
KENDE, H. : 124.
KENNEDY, I.R. : 354.
KHAN, A.A. : 439, 443, 451, 674, 1316, 1317.
KHAN, M.I. : 675.
KHANDUJA, S.D. : 691, 692.
KHAVKIN, E.E. : 676, 1483.
KHAZOVA, I.V. : 219.
KHUDTAKOVA, G.M. : 607.
KIDD, A. : 426.
KIELISZEWSKA-ROKICKA, B. : 677.
KIHARA, H. : 678.
KIM, S.S. : 679, 680.
KIMURA, H. : 1266.
KIMURA, S. : 681.
KINDL, H. : 681a.
KING, C.M. : 87, 88.
KIRAN, U. : 8.
KITAMURA, 1. : 598, 599, 903.
KITAOKA, S. : 1207.
KLEBANOFF, S.J. : 89, 537, 538, 634, 635, 1122a.
KLEIN, D. : 592.
KLISURSKA, D.Y. : 310, 311, 682.
KLUSAK, H. : 91, 683.
KNAB, R. : 565.
KNAPP, A.G. : 867.
KNUUTTILA, M.L.E. : 1319.
KNYPL, J.S. : 684.
KOBREHEL, R. : 619, 685, 686, 687, 688.
276 PEROXIDASES 1970/1980
KOBYL'SKAYA, G.Y. : 689.
KOCH, H. : 475, 476, 477, 478.
KOCHBA, J. : 360, 690, 1252.
KOCHHAR, S. : 691,692.
KOCHHAR, Y.K. : 691, 692, 932.
KOENIGS, J.W. : 693, 694.
KOHLER, B. : 695.
KOKKINAKIS, D.M. : 696, 697.
KOLEK, J. : 1056.
KOMARYNSKY, M. : 1188.
KONZE, J.R. : 697a.
KOSMAN, D.J. : 1339.
KOSSATZ, Y.c. : 698.
KOSULINA, L.G. : 1050.
KOYACS, 1 : 699.
KOYACS, K. : 330, 508.
KOYALEYA, L.U. : 689.
KOZHANOYA,O.N. : 1126.
KRASNUK, M. : 700.
KRAUT, J. : 1051.
KREMER, D.F. : 263.
KREMER, M.L. : 701.
KRENZ, J. : 465.
KRINSKY, M.M. : 702.
KRISNANGKURA, K. : 703
KRISPER, J. : 704.
KROBER, H. : 982.
KRGER, G. : 705.
KRUGER, J. E. : 706, 707, 720, 721.
KRUSBERG, L.R. : 595.
KRZYWANSKI, Z. : 1294.
KU, H.S. : 708, 709.
KUEHL, FA : 710.
KUHLMANN, W.D. : 711.
KUHN, C.W. : 81.
KUHNS, Ll. : 712, 713.
KUMAR, A. : 613a.
KUMAR, D. : 714.
KUMAR, S.A. : 647, 648, 1157.
KUMLIEN, A. : 121, 185, 715.
KUNISHI, A.T. : 763.
KURAOKA, T. : 716.
KURILlNA, TA : 1359.
KUTACEK, M. : 669.
KUYPERS, H.G. : 717.
KWIEK, S. : 718.
277 AUTHOR INDEX
LABERGE. D.E. : 706,707.719.720. 721.
LACROIX. Ll. : 886.
LAOONIN, V.F. : 722.
LADYGINA, M.E. : 1127.
LAGROU. A : 320.
LAIGNELET, B. : 688.
LALORAA, M.M. : 99a, 723, 855, 856, 857.
LAM, TH. : 723a.
LAMAISON, J.L. : 724.
LA MAR, G.N. : 724a.
LAMBERT, N.J. : 962.
LAMOND, M. : 144.
LAMPORT, D.T.A : 725, 768, 769.
LANDEGREN, V. : 24.
LANE, F.E. : 169.
LANE, N.J. : 726.
LANGOWSKA, K. : 462.
LANGRY, K.C : 724a.
LANIR, A : 727, 1162.
LATZKO, F. : 673.
LAU, O.L. : 728.
LAUREMA, S. : 729.
LAVANCHY, P. : 1038.
LAVARENNE, A : 140.
LAVEE, S. : 690, 729b, 1215.
LAZAR, G. : 729a.
LEAL, A : 307.
LEATHER, G.R. : 2, 255.
LEBEDEVA, O.V. : 730,731,732, 1359, 1360.
LEE, K.C : 733, 760, 761, 1273.
LEE, R.F. : 631.
LEE, TT : 734,735,736, 737, 738, 739, 740, 741, 742, 743, 744.
LEFF, P. : 70.
LEGG, P.G. : 1452.
LEGRAND, B. : 745,746,747,748,749,750, 1017, 1398.
LEIGH, J.S. : 751.
LENHOFF, H.M. : 943.
LENNA, D. : 17.
LEON, A. : 186.
LEPP, N.W. : 244
LESCURE, AM. : 752, 952.
LESHEM, Y. : 753, 754.
LESLlE, B.A. : 1061.
LEV, S.L.K. : 755.
LEVER, W.F. : 971.
LEVIN, S. : 380.
LEVINGS, CS. : 756.
278
PEROXIDASES 1970/1980
LEW, J.Y. : 757, 1208.
LEWAK, S.T. : 353, 758. 1135, 1320.
LEWIS, D.H. : 184.
LHOSTE, A.M. : 759.
LIANG, G.H. ; 259, 733. 760. 761.
LIANG, Y. T. : 761.
LlBERMAN-MAXE, M. ; 762.
LlEBERMAN, M. : 763 ..
LlEM, H.H. : 764.
LlUEGREN, D.R. : 765.
LlNDBECK, G. : 284.
LlNSMAIER-BEDNAR, E.M. : 87, 88.
LORET, C : 171.
LlPETZ, J. : 766.
LIS, E.K. : 1134.
LITT, M. : 248.
LIU, E.H.. 463, 464, 766a, ;67. 768. 769.
LlVSHITZ, NA : 1199.
LO, S. : 1173.
LOBARZEWSKI, J. : 770, 771, 772.
LOCKHART, B.E. : 773.
LOEBENSTEIN, G. : 1267.
LOEMOSZEWSLA-ROKICKA, B. : 774.
LOEPFE, E. : 393.
LOEWENBERG, J.R. : 209.
LOH, J.W.C : 775.
LOH, P. : 362.
LOPEZ-GORGE, J. ; 306, 307.
LOUIS, J.P. : 646, 776.
LOUW, A. : 1396.
LOW, L.E. : 611.
LOY, J.B. : 777.
LU, A.T. : 778.
LUCK, CD. : 667.
LUDDEN, P. : 271. 271a.
LUNDQUISI, 1. : 779.
LYLE, B.J. : 667.
LYSOV, Y.P.: 1199.
LYTTLE, CR. ; 317, 780, 781, 782, 976.
AUTHOR INDEX 279
MA, M. : 959.
MAC CAY, P.B. : 783.
MACCECCHINJ, M.L. : 783a.
MACCLURE, J.W. : 122.
MAC COWN, B.H. : 515a, 784.
MAC COWN, D.D. : 784.
MAC CREIGHT, W.H. : 785.
MACDONALD, T. : 786.
MACHACKOVA, 1. : 787, 788, 1487.
MACHEIX, J.1. : 1043a.
MACIEJEWSKA-POTAPCZYKOWA, W. : 789, 790.
MACKEEVER, P.E. : 791.
MACKO, V. : 792.
MACLACHLAN, T. : 868.
MACMILLAN, e. : 793.
MACNABB, T. : 794,795.
MACNICOL, PX : 796, 797.
MACPHIE, J.L. : 798.
MACRIS, B.J. : 799.
MADER, M. : 800, 801, 802, 803, 804, 805, 806, 807, 808, 942.
MAEDA, M. : 34, 904.
MAGE, M. : 318.
MAGEE, W.E. : 809.
MAGONOW, S.N. : 810.
MAGRO, P. : 17.
MA1ER, R. : 811.
MAILLARD, F. : 812.
MAISKY, V. : 717.
MAHADEVAN, S. : 647, 648.
MAKINO, R. : 813, 814, 815, 816, 1454, 1460, 1460a.
MALDONADO, BA : 813a.
MALHOTRA, S.K. : 1247.
MALHOTRA, S.S. : 1247.
MALIK, e. P. : 324, 816a.
MALOOF, F. : 288, 937.
MALTEMPO, M.M. : 751,817.
MANES, M.E. : 818.
MANIGAULT, P. : 287, Il 24a.
MANTLE, D. : 289.
MAPSON, L.W. : 819, 820, 821.
MARAITE, H. : 822.
MARANI, E. : 823.
MARAVOLO, N.e. : 1250.
MARCHESINI, A. : 1187.
MARCU, Z. : 146a, 254, 914, 1223.
MARCUS, A. : 824.
MARCUS, Z. : 1043.
MARIE, J.P. : 825.
----
280 PEROXIDASES 1970/1980
MARIGO, G. : 331.
MARIGOLIASH, E. : 941.
MARINESCU, M. : 229.
MARKAKIS, P. : 799.
MARKLUND, S. : 826, 827, 828.
MARKOTAI, J. : 1129, 1130.
MARKS, M.E. : 162.
MARKWALDER, H.U. : 828a.
MARR, e.D. : 829.
MARRA, C.M. : 667.
MARRUCCHINI, e. : 1307.
MARSALEK, L. : 830, 831.
MARSHALL, D.R. : 832, 833.
MARSHALL, M. : 498.
MARTE, M. : 890.
MARTH, E.H : 332.
MARTIN, e. : 178.
MARTIN, J.e. : 505.
MARTIN, S.M. : 880.
MARTINEZ, J. : I043a.
MARTINO, E. : 138.
MARTY, F. : 834.
MARTYUCHENKO, S.A. : 835.
MARUYAMA, T. : 836.
MASIAKOWSKI, P. : 1441.
MASON, D.Y. : 837.
MASSEYEFF, R. : 326.
MATEESCU, MA : 838, 1163.
MATHUR, S.N. : 1115.
MATHYS, W. : 839.
MATILE, Ph. : 486, 840.
MATKOVICS, B. : 330, 508, 1220.
MATKOVICS, 1. : 330, 508.
MATO, M.e. : 841, 842, 843.
MATSUNO, H. : 844.
MATTA, A. : 458.
MATTHEW, lA. : 423.
MATTHEWS, P. : 845.
MATTOO, A.K. : 846, 847.
MAUCHAMP, J. : 1084.
MAYBERRY, J.S. : 848.
MAYBERRY, M. : 940.
MAZAU, D. : 849, 850.
MAZZA, G. : 555, 851, 852, 853, 854, 1102, 1425, 1438.
McGALDRIE, T. : 1278.
McGEER, E.G. : 1266.
McLEESTER, R.e. : 515a.
MECHAM, D.K. : 371.
i
~ ...
281 AUTHORINDEX
MEIXALF, D.G. : 7.
MEERABAI, A. : 1297a.
MEGHA, B.M. : 855, 856, 857.
MEHTA, S.L. : 1075, 1230.
MENDEZ, J. : 843, 1029.
MENDGEN, K. : 858, 859.
MENEGHINI, R. : 860.
MENNES, A.M. : 861,862,863,979.
MENZEL, D. : 864, 865.
MEREDITH, W.O.S. : 721.
MERRETT, M.J. : 166.
MERZLYAR, M.N. : 45.
MESULAM, M.M. : 866, 867.
METZLER, M. : 868.
MEUDT, W.J. : 869, 870.
MEYER, H.E. : 522.
MEYER, Y. : 804, 805.
MIA, AJ. : 1073.
MIASSOD, R. : 871, 1028.
MICHAELS, AW. : 83.
MICHELSON, A.M. : 1057.
MICHOT, J.L. : 872.
MIGLER, R. : 873.
MIKILA, J.J. : 43.
MILDVAN, AS. : 492.
MILEWSKA, E. : 789.
MILLER, A. : 115.
MILLER, F. : 560, 561, 562.
MILLER, GA : 874.
MILLER, R.L. : 1282.
MILLER, R.W. : 875, 876, 1233.
MILLS, R.R. : 284.
MILNE, D.L. : 877.
MINEYEV, A.P. : 1199.
MINOCHA, S.c. : 521,878,879.
MISAWA, M. : 880.
MISHRA, D. : 657, 998.
MISRA, H.P. : 881.
MITRA, R. : 882, 883.
MITSUI, T. : 884.
MIYOSHI, K. : 1460a.
MLODZIANOWSKI, F. : 1044, 1246.
MOCHAN, E. : 885, 944.
MODESTO, R.R. : 236.
MODI, V. V. : 846.
MOHR, P. : 1091, 1092.
MOLLENHAUER, H.H. : 184.
MOLNAR, J.M. : 886.
PEROXIDASES 1"970/1980 282
MOLOKOV, L.G. : 887.
MONAKHOVA, O.F. : 1050.
MONGET, D. : 888.
MONTALBINI, P. : 889, 890.
MONTIES, B. : 192, 8903.
MOORE, A.L. : 1103, 1104.
MOORE, R.M. : 259, 733.
MOORE, T.S. : 891.
MOREAU, J.N. : 1397.
MOREAU,M. : 193,266, 335, 336, 483, 1058.
MORELL, D.S. : 893.
MORFAUX, J.N. : 1397.
MORGAN, P.W. : 398, 894, 895.
MORIKAWA, T. : 896,
MOSER, H.L.A. : 1068.
MORISHIMA, 1. : 897, 898, 899, 900, 966,
MORITA, H. : 876.
MORITA, Y. : 598, 599, 901, 902, 903, 904, 1315, 1475.
MOROT-GAUDRY, J.F. : 335,336.
MORRIS, G. : 905.
MORRIS, R. : 1325.
MORRISON, M. : 83, 84, 85, 272, 906, 907, 908, 909, 1442.
MORTON, T.C. : 540.
MOSS, M.B. : 867.
MUCCHIELLl, A. . 326.
MUELLER, W.C. : 910.
MUFSON, E.J. : 867.
MUJER, C.V. : 9103.
MUKHERlEE, S. : 102, 103, 911.
MUKHERlI, S. : 912, 913, 999.
MULLER, W.H. : 615.
MULLER-EBERHARD, V. : 764.
MULLIGAM, R.M. : 529.
MUMFORD, L.M. : 963.
MUMMA, R.O. : 522.
MUNCH, P. : 806.
MURESAN, T. : 914.
MURPHY, C.F. : 756.
MURPHY, M.J. : 915,916,917,918.
MURR, D.P. : 728.
MUSSELL, H.W. : 9183, 1283, 1284.
MUSTACCHI, P. : 145.
MYRZAEVA, S.V. : 919.
i
283 AUTHOR INDEX
NADEZHDIN, A. : 920, 920a.
NAOOLNY, L. : 921.
h : ~
NAFICHI, N.E. : 1367. ~ : : . : : :
NAGAO, M. : 1149.
NAGASAKA, A. : 922.
NAGLE, D. : 1422.
NAGLE, N.E. : 923.
NAINAWATEE, H.S. : 212, 649.
NAIK, M.S. : 1153.
NAITO, N. : 1458.
NAKAGAWA, H. : 969.
NAKAI, Y. : 663.
NAKAJlMA, R. : 924, 925, 1460a, 1463.
NAKAMURA, C. : 288.
NAKAMURA, Y. : 926.
NAKANISHI, S. : 927.
NAKANO, Y. : 1207.
NAKATANI, H. : 900, 928.
NANDA, J.S. : 207.
NANDA, K.K. : 100, 101,213,214,215,323,493,930,931,932,933, 1157.
NANDI, B. : 206.
NANDRIS, D. : 455.
NASINEC, V. : 788.
NASSIF-MAKKI, H. : 242.
NATARELLA, N. : 934,935.
NAVASERO, E.P. : 936.
NEARY, J.T. : 288, 937.
NEGRUTlU, I.: 180, 181,938.
NELSON, E.C. : 939, 940, 941.
NEMCSOK, J. : 581.
NESSEL, A. : 807, 942.
NEUCERE, N.J. : 1322.
NEUHAUSSER, E.F. : 529.
NEUKOM, H. : 828a.
NEUMANN, H. : 360
NEWCOMB, A.M. : 622.
NEWCOMB, W. : 653.
NEWELL, PA : 329.
NGO, T.T. : 943.
NICHOL, A.W. : 893.
NICHOLlS, P. : 885.
NICHOLLS, P. : 944.
NICOLAE, S. : 15.
NICULESCU, S. : 229, 605.
NIEDERMEYER, W. : 945.
NIEMTUR, S.T. : 946.
NIKAIDO, H. : 599.
NIKOLAEVA, M.G. : 947.
NIKOLOV, S. : 948.
284 PEROXIDASES 1970/1980
NIR. 1. : 949.
NISH1YAMA. F. : 1471.
NOBLE. R.W. : 950.
NOGUCHI, M. : 1210. 121 J. 1212.
NORMAN, T. : 25.
NORRIS. S.H. : 236.
NORTHCOTE. D.H. : 503. 1478.
NORTON. W.T. : 183.
NOUGAREDE. A. : 951. 952.
NOVACKY. A. : 953, 954.
NOVAK. J.F. : 955, 956.
NOVIKOFF, A.B. : 957, 958, 959.
NOVIKOFF, P.M. : 958, 959.
NOVITSKI, M. : 164.
NUMEZ, J. : 872, 1412.
O'BRIEN, C.R. : 960.
O'BRIEN, J.S. : 1039.
O'BRIEN, P.J. : 474, 589, 590, 960, 961, 1035, 1308.
O'BRIEN, T.P. : 1241.
OBST, Y.R. : 525.
OCHIAI, H. : 1205.
OCKERSE, R. : 962, 963, 964.
O'CONNOR, M.N. : 548.
ODAJIMA, T. : 965.
ODOARDI, M. : 987, 1248, 1249.
OERTLI, J.J. : 395.
OGAWA, S. : 897, 898, 899, 900, 966.
OGISO, K. : 1301.
O'HEOCHA, C. : 915, 916, 917, 918.
OHGUCHI, T. : 967.
OHKAWA, K.I. : 31, 970.
OHLSSON, P.J. : 220, 751, 817, 828, 968, 1002, 1003, 1004.
OHRMAN, B..: 1005.
OHTAKl, S. : 969.
OKA, H.I. : 984.
OKUN, M.R. : 971, 997,1132.
OKUNO, Y. : 972.
OLIVEIRA, O.M. : 86, 228.
OLSEN, J.L. : 973.
OLSEN, L.F. : 974, 975, 975a.
OLSEN, R.L. : 976.
OLSON, A. : 976a.
OLTEANU, G. : 459.
OMRAN, R.G. : 977.
k>
l',':....
285 AUTHORINDEX
ONG, H. T. : 978.
OOSTROM, H. : 863, 979.
OPARA, A. : 828.
ORTEGA, E.I. : 980.
OSBORNE, D.J. : 981,1108,1109,1110,1154,1155.
OSHINO, N. : 362.
OSSELTON, J.e. : 823, 1111.
OSTY, J. : 872.
OR, N. : 971.
ORY, R.L. : 210, 211.
OVCHARENKO, GA : 607, 1012.
OZEL, M. : 982.
PADMA, A. : 983.
PAl, e. : 984.
PALFI, G. : 322.
PALMER, e.E. : 985.
PALMIANO, E.P. : 986.
PALMIERI, S. : 987.
PANDEY, R.L. : 490,
PANTEL, S. : 988.
PAPADIMITRIOU, J.M. : 989, 1117.
PARISH, R.W. : 990, 991, 992, 993, 994.
PARK, K.H. : 995.
PARTRIDGE, J.E. : 996.
PARUPS, E.V. : 875.
PASMAN, A.J. : 1143a.
PATEL, e.S. : 536.
PATEL, R.P. : 997, 1132.
PATEL, V. : 273.
PATRA, H.K. : 998.
PATRIARCA, P.e. : 998a.
PAUL, A.K. : 999.
PAUL, B.B. : 611,1000,1001.
PAUL, K.G. : 220, 751, 817,828,968, 1002, 1003, 1004, 1005, 1006.
PAULSEN, G.M. : 733.
PAULUS, K. : 339.
PAWAR, V.S. : 1007.
PAYNE, M.G. : 1079.
PEDERSEN, M. : 1009.
PEIRCE, L.e. : 1010.
PElVE, Y.V. : 608, 1011, 1012, 1013.
PELLINIEMI, L.J. : 1014.
PENEL, CI. : 135a, 282, 444, 445, 479, 658, 659, 660, 661, 749,1015, 1016, 1017,
1018, 1019, 1021, 1022, 1023, 1024, 1025, 1026.
286
PEROXIDASES 1970/1980
PENNEY, G.O. : 1027.
PENON, P. : 871, 1028.
PEREIRA, J.R. : 1029.
PERESSE, M. : 193, 423a, 266, 484.
PEREZ DE LA VEGA, M. : 95.
PERL, M. : 1096, 1097.
PERLEY, J.E. : 785.
PESCE, AY. : 236.
PESCI, P. : 1400.
PETCULESCU, : 176.
PETER, R.. : 553.
PETERSSON, L. : 817.
PETZOLD, H. : 982.
PFE1L, E. : 705.
PFLUG, W. : 1029a.
PHAN, C.T. : 1030.
PHELPS, C. : 1032, 1033, 1034.
PHILLlPS, D.R. : 423.
PHlPPS, DA : 244.
PHIPPS, J. : 174, 1034.
PIATT, J. : 1035.
PICKERING, J.W. : 1036, 1054.
PIEFKE, J. : 462.
PILET, P.E. : 485, 742, 812, 1037, 1038.
PILZ, H. : 1039.
PINCKARD, JA : 1417.
PINCUS, S.H. : 1040.
PINGEL, U. : 1041.
PINO, R.M. : 1042.
PIRRWITZ, J. : 1092.
PIRVU, T. : 146a, 1043.
PITTS, A : 1421.
PLACHY, C. : 1176.
PLAPINGER, R.E. : 1184.
POSSEL, J.L. : 1043a.
POH-FlTZPATRICK, M.B. : 764.
POLEVOl, V.V. : 689.
POLlTYCKA, B. : 1044.
POLLAK, V.E. : 236.
POMMIER, J. : 1412.
POOVAIAH, B.W. : 1045, 1046, 1047, 1048.
POPOV, D. : 13.
PORTSMOUTH, D. : 1049.
POTAPOV, N.G. : 1050.
POTTY, V.P. : 636.
POU LOS, T.L. : 1051.
POURRAT, A : 724.
POURRAT, H. : 724.
POUX, N. : 1052, 1053.
287 AUTHOR INDEX
POWELL, B.L. : 1036, 1054.
PRASAD, R. : 1200.
PRASAD, S. : 1247.
PRATT, H.K. : 708, 709.
PRATT, J.M. : 6.
PRETLOW, T.G. : 162, 1421.
PRETORIUS, W.J. : 1392.
PRONINA, N.B. : 722.
PRZYBYLSKA, J. : 1055.
PSENAKOVA, T. : 1056.
PUCHALSKI, J. : 1144, 1145.
PUFF, C. : 704.
PUGET, K. : 1057,
PUGIN, A. : 336, 423a, 1058.
PUJARNISCLE, S. : 253.
PULITI, R. : 1188.
PULLMAN, H. : 1345.
PUPPO, A. : 1059.
PUROHIT, S.D. : 1060, 1060a, 1060b, lO73a, 1073b.
PUTNEY, J.W. : 1061.
PUXEDDU, P. : 1114.
QUAIL, P. : 1062.
QUALSET, C.O. : 1226.
QUINANA, N. : 957, 958, 959.
QUOIRIN, M. : 1063.
RAA, J. : 356, 1064, 1065, 1066, 1067.
RACKIS, J.J. : 1068.
RADOLA, B.J. : 298, 299, 300, 301, 302, 303, 304, 1068a, 1131.
RAHlMTULA, A.D. : 961.
RAJHATHY, T. : 378a.
RAKADJIEVA, D.L : 58a.
RALSTON, J. : 1069.
RAM, C. : 59, 60, 61, 62, 1070, 1071, 1072.
RAMAIAH, P.K. : 1073.
RAMAKRISHNAN, T. : 319.
RAMAWAT, K.G. : 1060, 1060a, 1060b, lO73a, 1073b.
RAMAZANOVA, L.K. : 1298.
RAMSEY, E.E. : 667.
RAMIREZ, DA : 910a.
288
PEROXIDASES 1970/1980
RANADIVE. A.S. : 1074.
RANJEVA. R. : 20.
RANSON, RJ. : 1441.
RAO. S.S. : 1189.
RAO, V.R. : 1075.
RAPPAPORT, L. : 1075a.
RASMUSSEN, L.F. : 163, 1045, 1046, 1047.
RATHMELL, W.G. : 1076, 1077, 1078.
RAUF, A. : 1078a.
RAUTELA, G.S. : /079.
RAWITCH, A.B. : 1080.
RAY, CG. : 89.
RAY, K. : 1080a.
RAY, P.M. : 373
RAYCHEBA, J. : 250.
REBAGAY, G.R. : 1203.
RECHTORIS, C : 1284.
REDDY, G.M. : 983.
REDDY, K.B.S.M. : 1279.
REDDY, M.M. ; 1081, 1082, 1083.
REGARD, E. : 1084.
REID, R. : 940.
REIGH, D.L. : 35, 1085, 1086, 1087, 1088.
REIMANN, L. : 1089.
REINER, A. : J090.
RENNERBERG, R. : 1091, 1092.
RENNERT, A. : 789.
RENNKE, H.G. : 1093.
RENWICK, J.A.A. : 792.
RETHORE, J.L. : 427.
RETIG, N. : 1094, 1095.
REUVENI, R. : 1096, 1097.
REYNOLDS, T. : 1098.
RHODES, J.M. : 1099.
RICARD, J.R. : 627, 628, 629, 852, 871, 1028, 1059, 1101, 1102,1438.
RICE, R.M. : 556.
RICH, P.R. : 1103, 1104.
RICHARD, L.B. : 547, 548, 552.
RICK, CM. : 1105, 1106, 1107.
RIDGE, 1. : 981, 1108, 1109, 1110.
RIETVELD, W.J. : 823, 1111.
RIGAUD, J. : 1059.
RINOONE, B. : 421a, 422.
RINEHART, R. : 35.
RITZERT, R.W. : 1113.
RIVA, A. : 1114.
RIZVI, S.J.H. : 1115.
ROBBINS, D. : 1116.
ROBERTSON, B. : 1067.
AUTHORINDEX 289
ROBERTSON, JA : 1117.
ROBINS, R.J. : 1117a.
ROCK, G.L. : 743.
RODRIGUEZ-KABANA, R. : 1348.
ROE, C.H. : 674.
ROELS, F. : 1118.
ROGAN, E.G. : 1119.
ROMAN, R. : 1120, 1121, 1122.
ROMER, D. : 459.
ROOS, D. : 131,269.
ROSEN, H.: 1122a.
ROSENSTOCK, G. : 1484, 1485.
ROSHCHUPKlNA, T.G. : 607.
ROSS, AF. : 1221, 1222.
ROSS, D. : 1433.
ROTH, R.W. : 1119.
ROTTLlO, G. : 1123.
ROUGE, P. : 1124.
ROUSSAUX, J. : 287, 1124a.
ROUTLEY, D.G. : 587.
ROZHKOVA, G.D. : 1358, 1361, 1362.
RUBERY, P.H. : 1125.
RUBIN, BA : 45,172,609,1126,1127,1128.
RUCHEL, R. : 175.
RUCKER, W. : 1129, 1130, 1131.
RUCKPAUL, K. : 1092.
RUDICH, J. : 1095.
RUDIN, Y. : 328, 783a.
RULE, AJ. : 1132.
RUNKOVA, L.V. : 1133, 1134.
RUSSO, J.F. :147.
RYAN, J.N. : 1446.
RYCHTER, A : 158, 758, 1135.
RZUCIDLO, L. : 718.
SACHAR, R.C. : 312, 1315.
SACHER, JA : 1136, 1137.
SACKSTON, W.E. : 238.
SADANAGA, K. : 1469, 1470.
SADANANDAM, A : 1297a.
SAE, S.W. : 1138.
SAFONOV, V. : 1139.
SAFONOVA, M. : 1139.
SAGI, F. : 419.
SAGIV, J. : 1140.
290 PEROXIDASES 1970/1980
SAHULKA, J : 1141.
SAIGO, S. : 678.
SAlTO, K. : 1235.
SAKURAI, N. : 1142.
SALAMINI, F. ; 987, 1248, 1249.
SALVATERRA, P.M. ; 1235.
SAMMONS, R. : 837.
SAMSHERY, R. ; 1143.
SANDERS, G.T.B. : 1143a.
SANIEWSKI, M. ; 1144, 1145, 1482.
SANO, H. : 1146, 1147, 1148, 1149.
SANO, T. : 900.
SANTIMONE, M. ; 1150, 1151, 1152.
SANTOS, S. : 164.
SARDHAMBAL, R.V. : 1153.
SARGENT, J.A. : 981, 1154, 1155.
SARKISSIAN, M.U. : 1164.
SARMA, TA ; 8.
SARRIS, J. ; 1397.
SASSER, J.N. ; 596, 597.
SAULESCU, N.N. : 14.
SAUTICH, MA : 216.
SAVAGE, N. : 240.
SAWADA, Y. : 1156.
SAWANO, F. ; 417.
SAWHNEY, N. ; 1157.
SAWHNEY, S.S. : 1157.
SBARRA, A.J. : 611, 1000, 1001.
SCALLA, R. : 178.
SCANDALIOS, J.G. : 30, 1158, 1159.
SCANNERINI, S. : 124a.
SCARPONI, L. : 1307.
SCHAEFER, H. : 1160.
SCHAEVERBEKE, J. : 208.
SCHAFER, P. : 1161.
SCHAFER, W. : 305.
SCHATZ, G. : 328, 783a.
SCHAUMBORG-LEVER, G. : 1132.
SCHE1D, B. : 957.
SCHEJTER, A. : 361, 727, 1[62.
SCHELL, H.D. ; 838, 1163.
SCHELLER, F. : 1091, 1092.
SCHERTZ, K.F. : 1164.
SCHIPPER, Jr. A.L. : 510, 1165.
SCHLEGEL, R. : 578.
SCHLOSS, P. : 808.
SCHMID, P.P.S. ; 1166.
SCHMIDT, G.M. ; 164, 1167.
SCHMIDT, H. : 1168.
AUTHOR INDEX 291
SCHMIDT-ULLRICH, B.: 1132.
SCHNEIDER, E.A. : 1169
SCHNEIDER, J. : 1170
SCHOKNECHT, J. : 809.
SCHONBAUM, G.R. : 492, 1089, 1172, 1173, 1427.
SCHOPFER, P. : 1174, II 74a, 1175, 1176.
SCHREIBER, W. : 1177, 1178.
SCHROEDER, W.A. : 197a.
SCHULTZ, J. : 381.
SCHULZ, H. : II 78a.
SCHUPPER, H. : 51 1.
SCHWACHHOFER, K. : 136,283..
SCHWAGER, H. : 672.
SCHWARZL, E. : 368.
SCHWENZER-RODRIGUEZ, N. : 1179.
SCHWIND, F. : 135.
SCOTT, K.M. : 1027.
SEEVERS, P.M. : 271, 271a, 1180, 1181.
SEIDLOVA, F. : 94.
SEKHON, A.S. : 1182.
SELIGMAN, A.M. : 949, 1183, 1184.
SELL, H.M. : 1467, 1468.
SELS, A.A. : 170.
SELVARAJ, RJ. : 1000, 1001.
SEMANCIK, J.S. : 773.
SEMENOVA, MA : 172.
SEN, S.P. : 103, 462a, 1184a.
SENGUPTA, B. : 1184a.
SENGUPTA, D.N. : 462a, 1184a.
SENGUPTA, T. : 1185.
SEQUEIRA, L. : 921, 1077, 1078, 1186.
SEQUI, P. : 1187.
SERY, T. : 511.
SESSA, D.J. : 1068.
SEVERSON, Jr. J.G. : 775.
SEVHONKIAN, S. : 1038.
SEVIER, E.D. : 1187a.
SEXTON, R. : 514, 515.
SGARAGLI, G. : 1188.
SHAILA, M.S. : 319.
SHANKARLINGAM, T. : 1189.
SHANNON, L.M. : 233, 757, 1187a, 1190, 1208, 1293.
SHANNON, M.C. : 1191.
SHANNON, S. : 1192.
SHANNON, Jr. W.A. : 1184.
SHAPIRO, B.L. : 26.
SHARMA, R. : 1193, 1194, 1195, 1196, 1197, 1198.
SHARMA, S.c. : 499.
SHARMA, V.K. : 490.
292 PEROXIDASES 1970/1980
SHARONOV, Y.A. : 810, 1199.
SHARONOVA, NA : 1199.
SHAW, C.R. : 1200.
SHAW, G. : 1278.
SHEEN, S.J. : 1201, 1202, 1203.
SHEID, B. : 957.
SHELTON, E. : 318.
SHEORAN, T.S. : 1204.
SHERI F, M. : 356a.
SHERWOOD, R.T. : 1370, 1371.
SHIBATA, H. : 1205.
SHIBATA, K. : 1142.
SHIGA, 1. : 1206.
SHIGEOKA, S. : 1207.
SHIH, J.H.C. : 1208.
SHIH, L.M. : 116, 754.
SHIMIZU, Y : 1409, 1486.
SHIN, W.Y. : 959.
SHINDLER, J.S. : 1209.
SHINSHI, H. : 1210, 1211, 1212.
SHIRINSKAYA, M.G. : 1012.
SHIRO, Y. : 966.
SHIV-PRAKASH, : 1153.
SHUMAKER, K.M. : 1213.
SHUSTERMAN, D. : 163.
SHUTOVA, E.A. : 216.
SIEGEL, B.Z. : 1214, 1215, 1273.
SIEGEL, S.M. : 1214, 1215, 1273, 1415.
SIES, H. : 562.
SILVEIRA, S.R. : 1216.
SILVERTEIN, R.M. : 505.
SIMOLA, L.K. : 1217, 1218, 1219.
SIMON, L.M. : 1220.
SIMONS, T.J. : 1221, 1222.
SINDILE, N. : 1223.
SINGH, D. : 1227, 1228, 1229.
SINGH, J.P. : 1153, 1224.
SINGH, M.P. : 1230.
SINGH, R.S. : 1225, 1226, 1227, 1228, 1229.
SINGH, T.G. : 1189.
SINGH, Y.D. : 99a.
SINGHAL, N.e. : 1230.
SINI(, Jr. K.e. : 934, 935, 1428.
SIRCAR, S.M. : 1185.
SIRJU, G. : 1231.
SIRKAR, S. : 1232.
SIROIS, J.e.L. : 876, 1233.
SITZMAN, E.V. : 941.
SKAKOUN, A. : 1234.
AUTHORINDEX 293
SLEMMON, J.R. : 1235.
SMAOUI, A. : 1236.
SMILLIE, L.B. : 1426, 1427.
SMINIA, T. : 161.
SMITH, D. : 446.
SMITH, E.C. : 679, 680, 755, 1036, l054, 1085, 1087, 1088, 1161.
SMITH, G.W. : 188.
SMITH, H. : 1237.
SMITH, H.H. : 222, 241, 574, 786, 1238, 1238a, 1239
SMITH, K.M. : 724a, 1240.
SMITH, M.D. : 809.
SMITH, M.H. : 1241.
SMITH, P.1. : 1242.
SMITH, R.L. : 1243, 1244.
SNYDER, E.B. : 1245.
SOBKOWIAK, A. : 1246.
SOKOLOVSKA, YA : 219.
SOLHEIM, B. : 1067.
SOLOMOS, T. : 1247.
SOLTANI, M.H. : 1402.
SOOBACK, M. : 288.
SOOST, R.K. : 365.
SOPANEN, T. : 1218, 1219.
SOPORY, S.K. : 613, 1194, 1195, 1196, 1197, 1198.
SORENSON, J.c. : 1159.
SORESSI, G.P. : 987, 1248, 1249.
SPAETH, S.c. : 1250.
SPENCER, D. : 420.
SPENCER, M. : 1247.
SPETTOLI, P. : Il, 1251.
SPICER, S.S. : 791, 1282.
SPIEGEL-ROY, P. : 177, 690, 1252.
SPIKES, J.D. : 654.
SPISUPALUCK, S. : 972.
SPRINZ, H. : 1253.
SPROOL, J. : 795.
SRIDHAR, R. : 1253a.
SRIVASTAVA, G.P. : 99.
SRIVASTAVA, H.S. : 1254.
SRIVASTAVA, K. : 47.
SRIVASTAVA, O.P. : 1255, 1256, 1257, 1258, 1259.
STAEHELlN, A. : 187.
STAFFORD, HA : 1260, 1261, 1262, 1263.
STAHMANN, MA : 309, 571, 1082, 1083, 1264, 1265.
STAINES, WA : 1266.
STARK, J.M. : 617.
STARRATT, A.N. : 744.
STASINOS, S. : 1279.
STECHER, K.J. : 870.
PEROXIDASES 1970/1980 294
STEELINK, C : 1476.
STE1GLEDER, G.K. : 1345.
STEIN, A. : 1267.
STEINER, H. : 347, 1268.
STEINMAN, RM. : 1269, 1270.
STEPHAN, D. : 1271.
STEPHENS, G.J. : 1272.
STEVENS, H.C': 1273.
STEWART, P.R. : 1437.
STEWART, R.R.C : 1274.
STIEBER, A. : 526.
STIGBRAND, T. : 220, 1006.
STILLMAN, J.S. : 347a, 1275, 1276.
STILLMAN, M.J. : 1275, 1276.
STOESSL, A. : 743, 744.
STONIER, T. : 480, 1277, 1278, 1279, 1280, 1281.
STOPPANI, A.O.M. : 138.
STOTZKY, G. : 640.
STOWARD, P.J. : 224,225, 1282.
STOWELL, CP. : 574.
STRAND, L.L. : 1283, 1284.
STRAUS, W. : 1285, 1286, 1287, 1288, 1289, 1290.
STRAUSS, R.R. : 611, 1001.
STRAUVEN, TA : 1295.
STREEFIRK, J.G. : 126, 989, 1292.
STREET, H.E. : 623.
STR1CKLAND, E. : 1293.
STROINSKl, A. : 1294.
STROUT, H.V. : 288, 937.
STRUM, J.M. : 1295, 1296, 1297.
STUART, M. : 1086.
STUBER, CW. : 756.
SUAREZ, S.J. : 359.
SUBHASH, K. : 1297a.
SUDERSHAN, : 8.
SUGAI, N, : 970.
SUKHORZHEVSKA1A, T.B. : 676.
SULEIMANOU, \.G. : 1298.
SUMPTER, NA : 1164.
SUTER1, B.D. : 1299.
SUZUK1, Y. : \300, 1301.
SVACHULOVA, J. : 1302.
SWAMY, G.K. : 1297a.
SWAN, GA : 1242.
SVRKOTA, B. : 1303.
SYMEONIDIS, L. : 1304.
SYONO, K. : 1305.
SYREN, E. : 1306.
SZWEYKOWSKA, A. : 1170, 1246.
AUTHOR INDEX
TAFURI, F. : 1307.
TAKAHASHI, M. : 41.
TAKANAKA, K. : /308.
TAKEO, T. : 1309.
TALWAR, S. : 613.
TAMURA, M. : /310, 1311, 1312, 1460a.
TAMURA, Y. : 1313.
TANAKA, S. : 31, 970.
TANAKA, Y. : 1314.
TANEJA, S.R. : 1315.
TANI, T. : 1458.
TAO, K.L. : 1316, 1317.
TARASEVICH, M.R. : 1465.
TAUROO, A. : 1080.
TAVASSOL/, M. : 764.
TAYLOR, D.D. : 1318.
TAYLOR, D.M. : 895.
TAYLOR, I.E.P. : J349.
TAYLOR,O.C. : 359.
TAYLOR, S.A. : 1357.
TEISSERE, M. : 871, 1028.
TENOVUO, J. : 1319.
TEPPAZ-MISSON, C. : 447.
TERNYNCK, T. : 160.
TERRANOVA, WA : 556.
TESTA-RIVA, F. : 1114.
TEWARI, M.N. : 59, 60, 61, 62, 63, 64, 65, 66, 1070, 1071, 1072.
THEVENOT, C. : 1320.
THIRUPATHAIAH, V. : 1189.
THOMPSON, K.R. : 1239.
THOMAS, D.L. : 69, 1321, 1322.
THOMAS, E.L. : 44, 1323, 1324.
THOMAS, JA : J325.
THOMAS, P. : 1326.
THOMAS, R.L. : 1326a.
THORNTON, J.D.. 410.
THORPE, TA : /34,446, 448, 1327, 1328.
THURLOW, M.D. : 329.
TING, P.L. : 481.
T1NGEY, D.T. : 1329, 1330.
T1RIMANA, A.S.L. : 1331.
T1XIER-VIDAL, A. : 1337.
TOBIN, c.L. : 500.
TODD, M.M. : 1332.
TOKUMASUS, : 664.
TOMARO, M.L. : 416.
TOMASZEWSKI, M. : 1134.
TONO, T. :418.
TORRES, A.M. : 1333, 1334, 1335.
; .
295
1
..
296 PEROXIDASES 1970/1980
TORREY, J.c. : 1336.
TOUGARD, C. : 1337.
TOURAINE, R. : 333.
TOWERS, G.J.N. : 1137.
TOWILL, L.R. : 209.
TRANTALIS, J. : 28.
TRAN THAN VAN, M. : 445, 448, 1328, 1345.
TRAVERS, F. : 1338.
THEHERNE, J.E. : 726.
TRESSEL, P. : 1339.
TREURNIET, F.E. : 863, 979
TRIPATHI, R.K. : 570, 1340, 1341.
TRIPPI, V.S. : 167,494, 1342, 1343, 1344, 1481.
TROJANOWSKI, J. : 772.
TRONSMO, A. : 1067.
TROST, T.H. : 1345.
TRUCHET, G. : 1346, 1347.
TRUELOVE, B. : 1348.
TSAY, R.C. : 1349.
TSEKOS, 1. : 1304.
TSIKOV, D. : 948.
TSUJI, A. : 34.
TU RCON, G. : 1382.
TURCU, A. : 1163.
TURIN, BA : 1113.
TURNER, P.T. : 1351.
TUTSCHEK, R. : 1352.
TYSON, H. : 384, 385, 386, 387, 388, 389, 390, 527, 1353, 1354, 1355, 1356, 1357.
UDA, H. : 836.
UEMOTO, S.c. : 652a.
UGAROVA, N.N. : 29,96, 730, 731, 732, 1358,1359, 1360, 1361, 1362.
ULIASZ, M. : 641.
UNGEMACH, J. : 808.
UNLUER, 0 : 78, 79.
URBAN, P. : 110.
URBANEK, H. : 790.
URITANI, 1. : 844, 1190, 1314, 1363, 1363a.
URS, N.V.R. : 348, 1364, 1365, 1366, 1366a.
1
AUTHORINDEX 297
VACCA, L.L. : 1367, 1368.
VACKOVA, K. : 669.
~ ~ ~ t ~
VALDVINOS, J.G. : 363, 554.
VAMOSVIGYAZO, L. : 1369.
VAN BERGEN-HENEGOUW, J. : 132.
VANBERKEL, T.J.C : 269.
VANCE, CP. : 1370, 1371.
VANDERMAST, CA. : 1372.
VANDERMEULEN, J. : 1118.
VAN DER PLOEG, M. : 1292.
VANDERRHEE, H.T. : 269.
VANDESTOUWE, R. : 1277.
VAN DE WALLE, CM. : 1061.
VANDUIJN, P. : 989.
VAN HAERINGEN, N.J. : 1373.
VAN HOOF, P. : 441,449, 1374, 1375.
VAN HOOF, R. : 292.
VAN HUYSTEE, R.B. : 182, 698, 813a, 1255, 1256, 1257, 1258, 1259, 1271, 1376,
1377, 1378, 1379, 1380, 1381, 1381a, 1382, 1403, 1404.
VANINGEN, E.M. : 11p.
VAN LELYVELD, U. : 269a, 637, 877, 1383, 1384, 1385, 1386, 1387, 1388, 1389,
1390, 1391, 1392.
VAN LOON, L.C : 1393, 1394, 1395.
VAN ZYL, A. : 1396.
VARDI, A. : 177.
VARFOLOMEEV, S.D. : 1465, 1466.
VARNER, J.E. : 30.
VAROQUAUX, P. : 1397.
VASILEVA, A.V. : 610.
VASIL'EVA, T.E. : 1362.
VASSEUR, J. : 750, 1398.
VAUGHAN, D. : 297.
VEECH, J.A. : 1399.
VEGETTI, G. : 1400.
VELAN, B. : 51 \.
VELEMINSKY, J. : 1302.
VENERE, R.J. : 140\.
VENKATACHALAM, MA : 1093, 1402.
VENNESLAND, B. : 642.
VER BEEK, R. : 413, 450, 451.
VERMA, D.P.S. : 1403, 1404.
VERMA, M.N. : 1340.
VERNANT, J.P. : 825.
. VERWOERD, N. : 1111.
VEST, G. : 1047.
VETTER, J. : 1405, 1406, 1407.
VICKERY, R.S. : 847, 1408.
298 PEROXIDASES 1970/1980
VlDIGAL, c.c.c. : 228, 350, 1409, 1410, 1486.
VlDIGAL-MARTINELLl, C. : 1411.
VIGIL, E.L. : 1332.
VILLIERS, EA : 877.
VIRION, A. : 1412.
, VIRON, A. : 711.
VOHRA, K. : 1341.
VORA, A.B. : 1413, 1414.
VORONKOV, L.A. : 1128.
VORONOVA, VA : 29.
VYAS, A.V. : 1414.
WABER, J. : 964, 1415.
WAHID, M. : 1416.
WAIGHT, R.D. : 70.
WAKS, M. : 16.
WALTERS, M.N.1. : 1117.
WANG, S.c. : 1417.
WARDALE, DA : 820, 821, 1418.
WATANABE, T. : 1419.
WEAVER, EA : 1239.
WEAVER, G.M. : 285.
WEBSTER, B.T. : 1420.
WEENING, R.S. : 1433.
WEIL, H.R. : 1345.
WEIR, E.E. : 1421.
WEISSMANN, G. : 1422.
WEISZ, H. : 988.
WELlNDER, K.G. : 853, 854, 1423, 1424, 1424a, 1425, 1426, 1427.
WELLBURN, A.R. : 579, 580, 1427a.
WELSH, H. : 553.
WENDER, S.H. : 679, 680, 755, 1036, 1054, 1087, 1088, 1161.
WENNBERG, R.P. : 163.
WERNER, D.J. : 1428.
WESTON, G.D. : 1429.
WETTSTEIJN, E.A. : 1430.
WEVER, R. : 131, 1433.
WHEELER, H. : 953, 954.
WHITAKER, D.R. : 778.
WHITMORE, F.W. : 1434, 1435, 1436, 1436a.
WICKLlFF, C. : 1329, 1330.
WIEBE, H.H. : 1048.
WIEGAND, N.K. : 1104.
WIGHTMAN, F. : 1169.
AUTHOR INDEX
. 299
WILLIAMS, B.J. : 1415.
WILLIAMS, E.E. : 1421.
WILLIAMS, H. : 845.
WILLIAMS, P.G. : 1437.
WILLIAMS, R.J.P. : 1102, 1438.
WILSKI, A. : 465, 1439.
WILSON, J.M. : 1440, 1448, 1449.
WILSON, L.A. : 601, 602, 603, 1231.
WILSON, M.T. : 1441.
WISE,B. : 1442.
WISSE, E. : 1118.
WITHAM, F.H. : 700.
WITTE, D.L : 1443.
WITTENBACH, VA : 1444.
WOCHOR, Z.S. : 1445.
WOESSNER, J.F. : 1446.
WOJCCHOWSKI, J. : 1294.
WOLFE, R. : 499.
WOLFFGANG, H. : 576.
WOLTER, K.E. : 1447.
WONG, E. : 1440, 1448, 1449.
WONG, Y.S. : 223, 1479.
WOOD, J.L. : 226.
WOOD, K.R. : 68, 1272, 1450, 1451.
WOOD, R.L : 1452.
WOODSON, G. : 1368.
WOOLTORTON, L.S.c. . 1099.
WORLEY, J.F. : 196, 197.
WOZNY, A. : 1044.
WRAY, P.H. : 1453.
WRIGHT, P.E. : 1438.
WRIGHT, R.D. : 70.
WYLER, R. : 393.
WYNDALE, R. : 452.
WYMAN, J. : 16.
WYSZOMIRSKA, J. : 718
YAKOVLEV, B.V. : 887.
YAMADA, H. : 533,813, 1454, 1455, 1456, 1460.
YAMAGUSHI, T. : 1457.
YAMASHITA, Y. : 1457.
YAMAMOTO, H.. 1458, 1474a.
YAMAZAKI, H. : 1461, 1463.
YAMAZAKI, I. : 33, 533, 534, 535, 606, 681, 813, 814, 815, 816,924,925,965,969,
1156, 1312,1454, 1455, 1456, 1459, 1460, 1460a, 1461, 1462, 1463, 1472.
300 PEROXIDASES 1970/1980
YANEZ. J. : 307.
YANG, H.M. : 1277, 1280, 1281.
YANG. S.F.. 708. 709, 728, 1464.
YAROPOLOV, A.1. : 1465, 1466.
YASUNAGA, T. : 900
YEH. R. : 1467, 1468.
YEN. S.T. : 1469, 1470.
YOKOTA. K.N. : 1462, 1463, 1472.
YOKOYAMA, M. : 836, 1471.
YONEDA, Y. : 1473, 1474.
YONETANI, T. : 252, 363, 1311, 1474a.
YONEZAWA, T. : 899,900.
YOSHIDA, C. : 902, 903, 904, 1475.
YOUNG, L.W. : 397.
YOUNG, M. : 1476.
YOUNG, 0 : 1477.
YOUSSEF, A.A. : 356a.
YUNG, K.H.. 223, 1478, 1479.
ZAAR, K. : 1480.
ZADEK, H.E. : 1344, 1481.
ZALEWSKA, J. : 790, 1482.
ZARSKA-MACIEJEWSKA, B. : 758.
ZEBA, B. : 1059.
ZELENEVA, I.V. : 1483.
ZENTMYER, GA : 655.
ZHIVOPISTSEVA, I.V. : 1128.
ZHIZNEVSKAYA, G.Y. : 1013.
ZHURKlN, V.B. : 1199.
ZIMMERMANN, H.J. : 1484, 1485.
ZIMNIAK-PRZYBYLSKA, Z. : 1055.
ZINNER, K. : 228, 350, 1409, 1410, 1411, 1486.
ZMRHAL, Z. : 787, 788, 1487.
ZOBEL, R.W. : 1107.
ZOHM, H. : 339.
ZOPPI, F. : 1488.
ZOTTER, M. : 369.
ZRYD, J.P. : 812.
ORGANISMIC INDEX
Abelmoschus esculentus : 8 16a
Abies sp. : 58a, 525, 640
Acacia koa : 10 10
Acer pseud"oplatanus : 191,265,623,670,672,752,812,951,952, 1218, 1429
Acer saccharum : 525
Achyranthes : 1060b
Actinidia sp. : 569, 570
Aegilops sp. : 786, 1304
Agropyron elongatum : 685
Agrostis tenuis : 839
Allium sp. : 467, 604, 1047, 1065
Alnus incana : 670
Amaryllis sp. : 1065
Amomum aromaticum : 998
Anagallis arvensis : 167
Ananas sp. : 877, 1388
Anthyllis vulneria : 342
Antirrhinum sp. : 1179
Arabidopsis thaliana : 181,938
Arachis hypogaea : 182,210,211,698, 813a, 998,1255,1256,1257, 1258,1259,1271,
1282, 1321, 1322, 1376, 1377, 1378, 1380, 1381, 1382, 1403, 1404
Argyranthemum : 704
Armoracia (see Cochlearia)
Asparagus officinalis : 444, 445, 449, 499, 1375
Atriplex halimus : 1236
Atropa belladona : 1217, 1219
Avena sp. : 21,22, 25, 234, 373,405,425,470, 523, 536, 756, 785, 832, 833,953,
954, 1080a, 1225, 1226, 1243, 1244, 1413, 1414, 1458, 1469, 1470
PEROXIDASES 1970/1980 304
Begonia evansiana : 1149
Beta vulgaris : 135, 173,242,325,433,435,441,459,990,991,992, 1079, 1251
Betula alleghaniensis : 473, 582, 586, 587
Boerhaavia diffusa : 998
Brassica japonica : 664
Brassica napus : 330, 555, 624, 626, 627,628,629,641,851,852,853,854,1102,1425,1438
Brassica sp. : 652a, 1064, 1066, 1126, 1223, 1273
Brassicoraphanus : 664
Bryonia dioica : 140, 141, 142, 143, 144
Bryophyllum daigremontianum : 1124
Calamagrostis villosa : 1178a, 1178b
Capsicum annuum : 330
Capsicum sp. : 1097
Chamaecyparis lawsoniana : 98
Chenopodium sp. : 71, 374,998, 1236
Chrysanthemum : 704
Cieer arietinum : 1078a, 1448, 1449
Cichorium intybus : 745,746,749,750,927, 1017, 1398
Citrullus sp. : 330, 1408
Citrus sp. : 177, 186, 330,360,365,418,442,690, 716, 1140, 1143, 1252, 1390, 1391
/ Coccini indica : 613a
Cochlearia armorica (= Armoracia lapathifolia) : 33, 182, 200, 220, 233, 236, 357, 486,
488, 489, 555, 605, 757, 768, 769, 817, 828, 1006, 1187a, 1423, /424,
1425, 1426, 1427, 1438
Cocos nucifera : 636, 910a
CofJea arabica : 480
Coleus blumei : 364, 556, 652
Cordia : 1073a
Crotolaria striata : 998
Cucumis mela : 822, 849, 850
Cucumi,\' sativus : 68, 99a, 123,330,356,615,789. 790,874,977, 1052. 1095, 1142.
1192,1303,1451,1452
Cucurbita maxima: 777, 1408
Cucurbita pepo : 251,313,330,352,777. 1024, 1025. \062
Cynara scolymlls : 650
Cyperlls rotllndlls 1060a
ORGANISMIC INDEX 305
Dactyli.r Klomerata : 1053
Datura sp. : 241, 286, 287, 383a, 494, 647, 648, 1124a, 1234, 1238a
Daucus carota . 115, 180, 521, 684, 1284, 1445
Deschampsia ./lexuosa : 1178a, 1178b
Diamhus caryophyllus : 190a, 191, 192, 193, 266, 423a, 483, 484, 784
Dionaea muscipula : 1Il 7a
Dioscorea composita : 1224
Eleusine corocana : 9518
Euphorbia characias : 834
Fagara coco: 495
FeslUca sp. : 330
Forsythia : 448a
Fragaria grandif/ora : 440, 1134
Fraxinus americana : 670
Fraxinus pennsylvanica : 525
Gibasis schiedicana : 1098
Gisekia : 1073b
Gladiolus sp. : 1065
Glycine max. : 18, 72, 81, 261, 263, 397,649,733,891,996, 1059, 1068, 1274, 1299,
1329, 1330, 1365
Gossypium hirsutum : 398, 894, 895, 910, 918a, 1232, 1283, 1284, 1399, 1401, 1417, 1442
306 PEROXIDASES 1970/1980
Helianthus annuus : 238, 330, 638, 639, 1083, 1278, 1280
Helianthus tuberosus : 76,77, 78, 79, 120,427,433,447,521,568,878,879
Hevea brasiliensis : J71, 253, 454, 455
Hibiscus sp. : 330, 998
Hordeum sp. : 21, 24, 25, 30, 53, 54, 58a, 59, 91, 122, 212, 244, 330, 340, 378a,
382, 406, 407, 450, 571, 575, 576, 683, 719, 720, 721, 722, 729, 883,
998, 1055, 1193, 1213, 1294, 1302
Hyacinthus orientalis : 1144
Hydrangea macrophylla : 886
Impatiens balsamina : 137,323,930, 1157
Ipomoea balalas : 108, 110, 115,498,600,601,602,603,844, 1190, 1231, 1314
Ipomoea fistulosa : 213
Lacluca saliva : 913
Lens culinaris (=Vicia lens) : 135a, 136,277,278,279,280,281,282,283,335,336,
337, 372, 411, 412, 413, 428, 432, 438, 439, 441, 443, 450, 451, 577,
674,842,843,871,1015, 1016, 1017, 1028, 1038, 1058, 1307
Lepidium salivum : 477, 478, 1480
Lilium longiflorum : 284
Linum usitatissimum : 384, 385, 386, 387, 388 389, 390, 510, 527, 1353, 1354, 1355,
1356, 1357
Lilchi chinensis : 637
Lupinus sp. : 93, 861, 862, 1050
Lycoper.l'icon esculentum : II, 13, 19, 92, 94, 148, 158, l72a, 216, 274, 330, 331,
356a, 359, 370, 399,458,468, 491, 572, 596, 696, 697, 708, 819, 820,
821, 847, 978, 987, 1010, 1094, 1105, 1106, 1107, 1248, 1249, 1297a,
1326a, 1418
ORGANISMIC INDEX 307
Mangijra indica : 205, 846, 1383, 1384
MattMola incana : 1133
Medicago sativa : 330, 700, 811
MelUotus alba : 618
Melilotus officinalis : 330
Mercurialis annua : 643, 644, 645, 646, 776
Mnium sp. : 58a
Musa sp. : 496, 500, 923
Nicotiana alata : 150, 151, 152, 153, 154, 155, 156, 157
Nicotiana glutinosa : 198
Nicotiana plumbaginifolia : 998
Nicotiana sp. : 1237
Nicotiana tabacum : 5, 9, 29, 75a, 88, 108, 109, 115, 116, 124, 134, 149, 174, 222,
223, 294, 295, 419, 445, 448, 521, 543, 544, 545, 546, 550, 552, 553,
554, 574, 596, 597, 665, 679, 680, 734, 735, 736, 737, 738, 739, 753,
754, 755, 759, 800, 801, 802, 803, 804, 805, 806,807, 808, 870, 921,
942, 948, 976a, 1031, 1036, 1054, 1077, 1078, 1081, 1087, 1088, 1113,
1127, 1129, 1130, 1131, 1161, 1201, 1202, 1203, 1210, 1211, 1212, 1221,
1222, 1239, 1267, 1305, 1327, 1328, 1344, 1393, 1394, 1395, 1406, 1407,
1430, 1478, 1479, 1481
Nicotiana xanthi : 178
Nuphar luteum : 172
Dryza sp. : 206, 207, 212, 358, 462a, 598, 599, 604a, 657, 887, 912. 936. 983. 984.
986,998,999, 1007, 1153, 1184a, 1185, 1253a
i
308 PEROXIDASES 1970/1980
Panicum mi/iaceum : 330
Papaver somniferum : 14
Parthenocissus tricuspidata : 522
Pelargonium sp. : 436, 521, 1048
Pennisetum typhoideum : 998
Persea americana : 158, 269a, 1333, 1334, 1335, 1385, 1386, 1387, 1389, 1392
Petunia sp. : 934, 935
Phalaenopsis amabilis : 1343
Phalaris arundinacea : 1370, 1371
Pharbilis ni! : 955, 1277, 1281, 1473, 1474
Phaseolus aureus : 8,62, 196, 197,312,404,728, 1103, 1143, 1204, 1341
Phaseolus mungo : 214,215,493,933
Phaseolus radiatus : 61, 1070, 10711
Phaseolus vulgaris : 36, 37, 38, 39, 40, 75, 146, 168, 260, 262, 285, 292, 330, 359,
501, 503, 514, 515, 581, 597, 775, 845, 858, 859, 880, 889, 890, 911,
956, 1045, 1076, 1220, 1342, 1348, 1400, 1420
Picea abies : 369, 482, 525, 672
Picea excelsa : 53
Picea glauca : 383, 525, 1349
Picea sp. : 923
Pinus banksiana : 1073
Pinus elliott : 1435, 1436a
Pinus nigra : 53, 58a, 670
Pinus palustris : 1245
Pinus radiala : 446
Pisum salivum : 21, 53, 54, 54a, 55, 56, 57, 58a, 59, 82, 113, [39, 147, 169, 188,
237, 258, 267, 268, 274, 275, 276, 297, 306, 307, 330, 373, 391, 392,
424, 441, 463, 547, 548, 549, 551, 588, 606, 6[6, 697a, 722, 796, 797,
841, 863, 919, 962, 963, 964, 979, 981, 1078a, 1082, 1108, 1109, 1110,
1139,1143,1146, J 148, 1154, 1155, 1247, 1301, 1346, 1347, 1372, 1397, 1482
Pinus sp. : 640, 670, 677, 774, 946, 1178a
Pinus strobus : 525, 670
Pinus ~ y l v e s l r i s : 43, 670, 946
Pinus laeda : 1245
Poinseuia : 1428
Populus deltoides : 469, 525
Populus niKra : 101,931,932
Populus sp. : 191,677,774, 1453
Populus lremuloides : 510, 525, 1165, 1447
1
ORGANISMIC INDEX 309
Prunus avium : 1046
Prunus persica : 396, 1043a
Prunus sp. : 444, 445, 1063, 1166, 1444
Pseudotsuga sp. : 640, 672
Pseudotsuga menziesii : 245, 632, 670
Pyrus communis : 158, 399, 400, 402, 1317
Pyrus malus: 125,353,471,525, 729b, 758, 947, 1135, 1320
Pyrus sp. : 1074
Quercus sp.: 670, 848
Raphanus sativus : 221, 592, 664, 902, 903, 904, 967, 998
Ricinus communis : 330, 1471, 1477
Robinia pseudoacacia : 591
Rosa: 712, 713
Rumex acetosa : 839
Saccharum o.fficinarum : 99
Salix sp. : 510, 5 15a
Salix tetrasperma : 100
Salvia splendens : 1133
Secale cereale: 330, 405, 578, 1075, 1298
Sedum album: 187a
Sifene alba : 747, 748
Sifene cucubalus : 839
Sifybum marianum : 475
Sinapis alba : 52, 573, 1174, 1174a, 1176
310 PEROXIDASES 1970/1980
Solalllllll IIIl.'lolIgl.'na : 330. 651
SolallulIl /uhl.'rosulIl : 127, 129, 130, 161, 218, 296,410,423,465,985, 1137, 1272,
1284, 1326, 1340, 1439, 1484, 1485
Sonlll.'ra/ia alha : 614
SOIhlls aucuparia : 525
Sorghlllll sp. : 330, 761, 765, 998, 1138, J164, 1262, 1263
Sparlina al/ernf/lora : 461 a
Spartina pans : 461 a
Spinacia sp. : 41, 305, 339, 414, 415, 444, 445, 479, 658, 659, 660, 661, 982, 1017,
1018, 1019, 1020, 1021, 1022, 1023, 1026, 1189
Syringa l'ulgaris : 525
Tabernaemomana coronaria : 998
Tagetes pa/ula : 1415
Taraxacum officinale : 675
Taxus cuspidata : 525
Thea sinensis : 1309, 1331
Theobroma cacao : 655
Thlaspi alpestre : 839
Tradescantia sp. : 1041, 1065
Trigonella foenum graecum : 60, 63, 64, 65, 66, 856, 857
Triticale sp. : 259, 760, 1075
Triticum aeslvum : 14, 15,21,23,95, 133, 146a, 189, 191, 199,201,203,264,270,
271, 271a, 330, 371, 394, 405, 409, 452, 506, 526, 578, 630, 631, 662,
683, 685, 686, 687, 699, 705, 706, 787, 788, 792, 835, 882, 998, 1043,
1180,1181,1227,1228,1229,1230,1241,1315,1316,1434,1487
Trilicum durum : 619,687, 1075
Tulipa sp.: 1145
Vlmus mOn/ana : 670
ORGANISMIC INDEX 311
Vaccinium corymbosum : 399
Vaccinium myrtil/us : 1178a, 1178b
Vaccinium vitis-idaea : 1178a, 1178b
Vicia faba : 502, 610, 1078a, 1141
Vicia sativa : 330
Vicia vil/osa : 330
Vigna mungo : 1115
Vigna sinensis : 773
Vigna sp. : 1279
Vitis sp. : 71, 691, 692
Xanthium pennsylvanicum : 209
Xanthium strumarium : 793
Zea mays : 10,17,53, 58a, 90, III, 114, 160a, 165,237,254,311,321,330.373,
395, 405, 425a, 425b, 434, 441, 485, 541, 613, 676, 682, 689, 742, 811,
830,831,914,949,980,993,994,998,1010,1056,1139, 1194, 1195,
1196, 1197, 1198, 1254, 1374, 1405, 1483
SUBJECT INDEX
Abscisic acid (elTect ot): 411, 412, 413, 439,716,855,1316.
Abscission : 2, 255, 442, 514a, 515, 543, 544, 545, 546, 550, 553, 554, 1045, 1046,
1097, 1384, 1420, 1444.
Acetylcholine: 1015, 1019, 1195.
Aging : 35, 112, 146, 149, 158, 167, 221, 457a, 471, 614, 642, 657, 659, 729a, 998,
1100, 1136, 1137, 1231, 1274, 1343, 1348, 1390, 1407.
Aigae : 7, 166,466, 563a, 864, 865, 915, 916, 917, 918, 1009, 1029, 1207, 1214.
Amino acid composition and sequence 680, 851, 853, 854, 902, 1423, 1424, 1425,
1426, 1427.
Anaerobiosis : 219, 328.
Anti-peroxidase : 132, 164, 187,236,490,837,972, 1006, 1167, 1235, 1270.
Apical dominance : 18.
Apo-peroxidase : 233, 327, 654, 680, 702, 709, 802, 853, 854, 902, 1034, 1093, 1293,
1362, 1423, 1424, 1424a, 1425, 1427.
Ascorbate peroxidase : 54a, 54b, 54c, 673, 1207.
Assay: 229, 239, 358, 377, 391, 421, 487, 558, 779, 838, 888, 943, 988, 1000, 1392.
Auxin (effect ot) : 42,66, 108, 115,222,267,268,278,281,309,337,360,372,428,
442, 450, 551, 588, 675, 689, 737, 748, 753, 754, 756, 812, 821, 871,
934,963,1071,1113,1155, 1219, 1405, 1406, 1429, 1434.
Auxin protectors : 213,427,436,456,480,497,684,744,934,955, 1041, 1142, 1233,
1277, 1278, 1279, 1280, 1281, 1305.
1
314 PEROXIDASES 1970/1980
Bacteria : 530, 1029a, 1037, 1324.
Bactericidal function : 48, 380, 634, 635, 865, 1001, 1122a, 1319, 1323, 1324, 1364,
1366, 1373.
Biosynthesis : 171, 267, 268, 532, 674, 757, 783a, 805, 824, 956, 1108, 1190, 1198,
1271, 1315, 1376, 1378, 1380, 1381, 1382, 1404, 1458.
- inhibitors : 76, 78, 114, 323, 581,954, 1108, 1190, 1198, 1381, 1382.
Bromoperoxidases 7, 50, 563a, 1009.
Browning: 637, 688, 1166.
Bryophytes : 460, 565, 612, 1044, 1170, 1246, 1250, 1352
Bud formation: 448, 569, 745, 750, 800, 806, 927, 938, 1327, 1328, 1398.
Calcium: 52a, 56, 133,352,454,530,619,966, 1016, 1024, 1061, 1424a.
Cal1us : 75, 75a, 181, 242, 448, 676, 690, 734, 735, 736, 737, 738, 739, 800, 806,
807,938,942,951, 1087, 1161, 1327, 1328, 1406, 1447.
Cancer: 240,316, 317,341,666, 1027.
Cel1 cultures: 36, 37, 38, 39,40, 74, 265, 414, 415, 623,676, 679, 680, 698, 747,
748,809,812, 813a, 880, 951, 952, 1036, 1054, 1112, 1113, 1210, 1211,
1212, 1217, 1218, 1219, 1255, 1256, 1257, 1376, 1377, 1378, 1380, 1381,
1382, 1403, 1404, 1429, 1483.
Cereal seeds : 212, 340,371,405, 598 599, 706, 707, 719, 720, 721, 729, 760, 761,
936,986, 1067, 1075, 1185, 1187, 1230, 1294, 1316.
Characterization : 7,4/, 247, 276, 319, 334, 345, 370, 385, 463, 528, 598, 605, 609,
610, 619, 650, 679, 68/, 682, 696, 828, 851, 873, 880, 901, 903, 904,
915, 923, 942, 980, 1006, 1080, 1103, 1128, 1138, 1146, 1209, 1211,
1240, 1259, 1352, 1369, 1459 1463.
Chemical studies : 6, 228, 308, 344, 361, 379, 461 a, 492, 533, 606a, 606b, 628, 731,
732, 813, 814, 815, 816, 872, 920, 925, 950, 968, 969, 1104, 1156, 1173,
1205, 1311, 1454, 1455, 1460, 1460a, 1462, 1474a.
SUBJECT INDEX 315
Chemical treatments : 52a, 54c, 122, 135, 136, 180, 181,215,3[0,324,549,775,877,
912,953, 1129, 1192, 1219, 1302.
Chemiluminescence : 34,45,291,511, 1057.
Chloroperoxidase : 246, 505, 1325.
Chloroplasts : 609,613,919, 1128.
Cold tolerance : 641, 700, 1194.
Coleoptile : 425, 470, 1431.
Compound J : 31a, 32, 106, 225a, 249, 289, 346, 347, 531, 534, 535, 563, 625, 626,
629,633,681,813,897,920,960,1004,1069,1120,1121, 1150, 1268,
1275, 1276.
Compound JI : 249, 256, 257, 331a, 347, 531, 534, 535, 897, 920, 920a, 960, 1121,
1122, 1276.
Compound JII : 33la, 429, 1033, 1312.
Crown-gall and other tumors : 9, 137, 260, 287, 524, 956, 1060, 1073a, 1073b, 1083,
1124a, 1125.
Cyanide : 250,347, 815.
Cytochemical.techniques : 10, 28, 31, 159, 179, 224, 225, 367, 376, 393, 487, 559,
561, 567, 711, 764, 779, 791, 866, 867, 884, 949, 958, 970, 989, 1014,
1090, 1118, [183, 1184, 1216, 1282, 1285, 1286, 1287, 1289, 1290, 1292,
1337, 1368, 1421.
Cytochrome c : 434,885,944, 1151, 1441.
Cytochrome c peroxidase : 170,252,328,362,363, 783a, 885, 941, 945. 1437.
Cytochrome P-450 : 354, 589, 590, 705, 961, 1091, 1092.
Cytokinins (effect of) : 38, 39, 40, 61, 66, 99a, 197, 278, 281, 337, 412, 439, 450,
521,588,734,737,739,749, 1129, 1170, 1193, 1316.
316 PEROXIDASES 1970/1980
2,4-D (effect of) : 38, 39, 40, 60, 180, 181,394,722,736,748,1005, 1113, 1253, 1429.
Development : 146,209,356,396,463,468,469, 572, 643, 720,847, 848,998, 1075,
1158,1220,1414.
Differentiation : 51, 52, 127, 128, 161,311,445,448, 462a, 503, 528, 569,612,644,
658, 800, 806, 878, 879, 927, 938, 1149, 1158, 1327, 1328, 1336, 1403,
1416, 1447, 1484.
Dormancy : 447, 452, 506, 691, 758, 936, 1047, 1317, 1320.
Dwarfism : 874, 1227.
Electrophoresis : 21, 130, 175,358,597,623,664,767,768,803,818,881,883,931,
1017, 1200, 1234, 1291, 1393.
Embryos : 443, 599, 758,947,959, 1135, 1317, 1320, 1445.
Endoplasmic reticu1um : 188, 191,265,320,467,515,544,952,959, 1024, 1381, 1420, 1480.
Ethylene (effect of) : 1,2, 5, 108, 110, 115, 188,218, 271a, 337, 364,442,498,499,
544, 545, 548, 550, 551, 552, 553, 554, 588, 600, 692, 716, 857, 894,
981,1030,1095,1109,1110,1155,1192.
- synthesis : 172a, 398, 571, 653, 697a, 708, 728, 762a, 763, 773, 788, 819, 820,
821, 1418, 1464.
Extraction: 294, 440,510,586,712, 723a, 738, 796, 813a, 937,1017,1171,1309,
1380, 1388, 1391.
Fern: 762.
Flowering : 444, 445, 448, 479, 658, 659, 1018, 1019, 1020, 1022, 1184a, 1328.
Fruit development and ripening : 125, 158, 396, 399, 400, 402, 471, 496, 500, 637,
705,708,720,721,846,847,923, 1068, 1075, 1383, 1384.
SUBJECT INDEX 317
Gene expression: 11,95, 157, l60a, 271, 271a, 420,578,685,686,786,984, 1007,
1107, 1164, 1180, 1237, l238a, 1315, 1470.
Genetics 13, 22, 23, 24, 25, 53, 58, 154, 165, 177, 211, 241,245, 254, 356a, 365,
378a, 382, 383, 383a, 384, 385, 386, 387, 388, 459, 460, 461, 494, 574,
652a, 761, 793, 797, 830 832, 874, 914, 934, 935, 939, 948, 983, 984,
1055, 1107, 1201, 1203,1223, 1226, 1237, 1238, 1245, 1254, 1304, 1333,
1334, 1335, 1354, 1355, 1356, 1357, 1428, 1469, 1470.
Geographical distribution: 254, 523,1105,1107, 1178a, 1178b,1213, 1225, 1349.
Gennination : 9, 30,43, 212, 312, 443, 452, 506, 649, 706, 986, 999, 1073, 1080a,
1185, 1187, 1204, 1227, 1228, 1229, 1247, 1294, 1320, 1322, 1342, 1477.
Gibberellins (efTect of) : 113,188,310,415,551,716,735,737,962,963,964,1022,
1071, 1133, 1157, 1316.
Glutathione peroxidase : 474, 516, 783.
Glycoprotein : 162,233,276,757, 1089, 1187a, 1376, 1424, 1425.
Golgi apparatus: 20, 1JO, 161, 191,265,467,515,1480.
Gradient in plants: 144,201,296,390,485,502,638,658, 1141, 1328.
Gravity (efTect of) : 504,524, 1415.
Growth 82, 149, 199, 202, 203, 208, 311, 321, 372, 373, 394, 424, 432, 433, 439,
450, 451, 502, 549, 615, 652, 761, 855, 947, 1015, 1071, 1072, 1088,
1142, 1154, 1155, 1192, 1405, 1406, 1416, 1447, 1453, 1483.
Growth retardants (efTect of) : 133,428,451,964, 1050, 1133,1141.
Halides 12, 85, 117, 118, 204, 246, 541, 593, 611, 627, 668, 715, 759, 906, 907,
908,909, 1035, 1040, 1062, 1084, 1120, 1122, 1268, 1323, 1324, 1412.
Herbicides: 122, 123, 1303, 1307.
Honnonal interaction: 18,66, 126a, 168,312,364,439,443,450,665,716,737,947, 1075a.
Honnones (animais) : 3, 26, 27, 67, 103, 175,227,240,316,341,621,622,666,667,
668, 780, 781, 782, 868, 1295, 1446.
Hybrids : 146a, 378a, 388, 830, 914, 1081, 1356, 1453, 1473.
318 PEROX1DASES 1970/1980
Hydrogen peroxide metabolism 158, 1220.
- formation: 138,357,488, 488a, 489, 517, 518,694,808, 1103, 1308.
Hydroxylation : 271b, 519a, 581, 606, 765,997, 1008, 1009, 1242.
Hydroxyproline : 283, 769, 850, 981, 1109, 1110, 1434.
IAA catabolism : 58a, 126a, 137, 168, 214, 237, 238, 244, 255, 274, 275, 336, 353,
356, 364, 373, 398, 399, 400, 406, 407, 411, 432, 436, 438, 458, 583,
587, 602, 612, 616, 632, 697, 742, 743, 773, 775, 789, 790, 812, 855,
856, 857, 861, 862, 895, 977, 987, 1018, 1041, 1050, 1056, 1064, 1141,
1149, 1169, 1231, 1372, 1398, 1429, 1439.
IAA oxidase isoforms : 169, 258, 269a, 470, 473, 584, 585, 677,734, 735, 736, 774,
818,931,962,1018,1038, 1080a, 1141, 1210, 1211, 1255, 1256, 1257,1474.
- localization : 91, 94, 134.
IAA oxidation : 90, 200,429, 430, 431, 437, 440, 456, 497, 522, 582, 601, 603, 697,
740, 741, 744, 752, 785, 787, 841, 842, 843, 852, 869, 875, 924, 933,
1066,1101,1134,1142,1148,1300,1371,1410,1461.
Immobilized peroxidases : 69, 73, 96, 1163.
Immunochemical studies : 46, 56, 57, 58, 182,286,287,645, 1124a, 1285, 1286, 1377.
Infection (reaction to) : 72, 81, Ill, 114, 173, 189, 205, 206,238, 260, 261, 266, 269a,
322, 335, 336, 407, 408, 409, 410, 423a, 425a, 425b, 454, 455, 458, 465,
482, 483, 484, 491, 498, 571, 595, 611, 617, 630, 631, 636, 655, 683,
792, 822, 835, 844, 849, 850, 858, 859, 889, 890, 918a, 967, 1058, 1060a,
J060b, 1082, 1097, 1126, 1127, 1153, 1165, 1180,1181, 1186, 1189,1224,
1253a, 1264, 1265, 1340, 1363, 1363a, 1364, 1366, 1366a, 1383, 1385,
1386, 1387, 1389, 1390, 1399, 1417, 1430, 1458.
Inflammation (animais) : 333, 710.
Inheritance : 756, 831, 1244, 1245, 1469.
Inhibitors 137, 197a, 288, 342, 464,476, 477, 478, 601, 619, 684, 744, 749, 826,
827, 1029, 1285, 1287, 1356, 1386, 1396.
Iodide peroxidase 85, 915, 922.
Ion deficiency 306.
SUBJECT INDEX 319
Ionie treatments (effect of) : 54, 54a, 54b, 55, 58a, 59, 141, 143, 186,244,308, 729b,
733,1013,1115,1468.
Irritation: 140, 141, 142, 143, 144, 148.
Isoelectric focusing : 258, 261, 298, 299, 300, 30 l, 302, 303, 584, 585, 803, 980, 1039,
1130, 1131, 1132.
Isoperoxidase patterns: 52, 53, 75, 75a, 116,125,172,311,313,338,365,381,389,
425, 470, 475, 494, 500, 502, 632, 640, 677, 774, 845, 903, 1054, 1098,
1298, 1331, 1355, 1474,
[soperoxidases in related species or cultivars : 14, 15, 22, 23, 24, 25, 182, 210, 211,
234, 241, 254, 259, 383a, 384, 494, 604a, 687, 704, 712, 713, 777, 833,
935, 1055, 1081, 1106, 1191, 1223, 1226, 1239, 1243, 1304, 1428.
Kinetics : 16, 33, 65, 70, 217, 257a, 289, 329, 343, 370, 531, 594, 629, 730, 752,
807, 933, 1033, 1056, 1066, 1085, 1088, 1121, 1122, 1150, 1359.
Lactoperoxidase : 197a, 907, 1003, 1062.
Leaf : 172, 174, 209, 221, 294, 321, 348, 369, 469, 650, 651, 658, 722, 948, 990,
991,998, 1031, 1236, 1298, 1331, 1398.
Light (effect of) : 54a, 92, 93, 122,292,613,745,746,749,755,784,799, 1137. 1193.
1229, 1237.
Lignification : 20, 139, 190a, 192, 487a, 499, 503, 507. 518, 525, 529, 564. 828a. 878.
879, 890a, 926, 967, 1074, 1099, 1214. 1261, 1370, 1371, 1436. 1436a.
Localization (animal cells) : 4, 28, 121, 184, 185, 248. 269, 293, 316, 366. 375. 417.
467, 468, 539, 557, 560, 662, 663. 714. 798. 823. 825. 836. 890. 957.
1042, 1114, 1116, 1296. 1297, 1351, 1419. 1452.
Localization (plant cells) : 94. 124a. 147. 155. 190. 190a. 191, 192. 193. 253. 264.
265, 266, 391, 392. 465. 513. 514. 515. 543. 544. 556. 645. 739. 762.
834, 858. 859. 863, 910. 919. 949, 951, 952. 979. 990. 991, 992. 1046.
1052. 1053, 1065,1246, 1262. 1399, 1402. 1408. 1420, 1442. 1480.
320
i
PEROXIDASES 1970/1980
Mechanisms of reaction : 90, 105, 106, 107, 195,231, 232, 249,250, 256, 257, 315,
347a, 422, 437, 453, 481,519,594,678,697,924,928, 1002, 1035, 1051,
1096, 1101, 1151, 1152, 1162, 1312, 1338, 1411, 1461.
Membrane-bound : 143,282,496,538,739, 847,951,952,991,992,993,994, 1016,
1023, 1024, 1372, 1381.
Mitochondria : 279, 434, 474, 864.
Molecular interactions: 6, 327, 625, 627, 702, 1002, 1162, 1172, 1456.
Morphactin (effect of) : 63, 930, 1072, 1482.
Mutants: 19,207,847, 910a, 987, 1145, 1179, 1248, 1249, 1297a.
Myeloperoxidase : 893, 965, 995a, 1122a, 1123, 1308.
Mycetes : 332,335,336,724,770.771,941, 1058, 1182, 1332, 1416.
Nitrate reductase activity : 31 a, 607, 608, 10 II, 1012, 1115, 1254.
Nuclear magnetic resonance : 724a, 727, 751, 897, 898, 899.
Nucleic acids : 87, 88, 621, 740, 753, 860, 956, 1409.
Nutrition: 98, 244, 307, 638, 733, 887, 895, 1115, 1140, 1273.
Oscillatory reactions : 291, 974, 975, 975a.
Ozone (effect of) : 262. 263, 285, 359, 1329, 1330.
SUBJECT INDEX 321
Peroxidase-like : 378,418,540, 701, 1049, 1440.
Pheno1ics : 74, 84, 297, 321, 389, 414,512, 519a, 547, 573,603,638,723,744,746,
787,795,856,876.996, 1060, 1099, 1100, 1134, 1142, 1148, 1161, 1177,
1178,1189,1202,1233,1258,1260,1261,1278,1281, 1314, 1366, 1418,
1435, 1440, 1476.
Photoperiod : 167,295, 462a, 1018, 1022, 1149, 1184a, 1413, 1453.
Phototropism : 504.
Physico-chemical studies : 225a, 492, 555, 563, 624, 654, 724a,751 , 810, 897, 898,
899,900,1147,1162, 1199, 1206, 1293, 1310, 1438, 1474a.
Phytochrome: 592,660,661,1019,1020,1023,1025,1174, 1174a, 1175, 1176, J 194,
1195,1196,1197,1198,1237.
Plant parts: 75, 75a, 135a, 494, 495, 502, 1139, 1344, 1442.
Plant selection: 165, 177, 1010, 1333.
Ploidy : Il, 338, 882, 896, 1043, 1238a, 1251, 1304.
Pollen tube: 149, 150, 151, 152, 153, 154, 156,284,324.
Pollution: 187a, 359, 395, 482, 509, 579, 580, 670, 671, 672, 733, 759, 811, 839,
911, 913, 946, 1048, 1178a, 1232, 1330, 1427a.
Proteins (etfect on) : 44, 183,309,457, 1062, 1436.
Protoplasts : 804.
Purification: 7, 17,41,47, 162, 230, 233, 272, 317, 319,326,619,650,696,794,
915,976, 1006, 1089, 1132, 1138, 1160, 1207, 1250, 1309, 1326a.
322 PEROXIDASES 1970/1980
Radiations uv : l72a. 501, 548. 553.
- x : 222.
- y : 1326, 1416.
Rapid effects : 660, 661, 1019. 1020, 1021, 1022, 1023, 1025, 1026.
Reactions catalyzed by peroxidases : 83, 84, 85, 86,97, 163,217,226,239, 271b, 273,
325, 349, 3 5 ~ 368, 4 2 1 ~ 422, 423, 4 5 7 ~ 462, 463, 481, 520, 566, 573,
605, 6[8, 647, 648, 656, 681a, 682, 703, 723, 730, 766a, 795, 828, 840,
872, 940, 971, 973, 1036, 1069, 1076, 1085, 1086, 1087, 1088, 1119,
Il 43a, 1177, 1178, 1188, 1202, 1215, 1339, 1440, 1443, 1448, 1449, 1457,
1467, 1472, 1486.
Resistance against infection: 13, 17,81,93,270,271, 271a, 355, 374, 575, 576, 889,
921,982, 1079, 1094, 1180, 1181, 1221, 1222, 1340, 1365. 1370, 1371,
1394, 1401, 1439.
Respiration: 500, 598, 599, 733, 999, 1390, 1406.
Ribosomes: 191,279, 428, 467, 952, 1028, 1066, 1480.
Root : 124a, 177,219,251,277,280,338,348,391,392,432,435,441, 502, 591,
615,616, 675, 742, 861, 862, 1141, 1187a, 1241, 1301, 1374.
- nodules: 861, 862, 863, 979, 1046, 1047, 1059, 1060, 1346.
Rooting : 100, 101, 120, 168, 196, 197,214,215,323,404,444,445,446,448,449,
493,568,652,886,930,931,932, 1041, 1063, 1217, 1328, 1375.
Secretion: 2, 135a, 227, 415,426,467,537,539,557,562,891, 976a, 1061, 1117a,
1382, 1480.
Seeds : 21, 330, 508, 640, 1043, 1078a, 1143.
Separation of isofonns : 162,233,381,384,397,679.
Sex expression: 613a, 643, 645, 646, 658, 659, 776, 790, 1018,1095, 1192.
Substrate specificity : 220, 605, 682, 1002, 1036, 1214, 1393, 1476.
Sulphydryl : 44, 61, 62, 64, 1070, 1071.
SUBJECT INDEX 323
Temperature (effect 01) : 135, 295, 306, 515a, 639, 641, 699, 700, 784, 977, 1124,
1182, 1227, 1317, 1321, .
Thermal stabi1ity : 29,96,223,303,304,305,339,778,802,995, 1056, 1313, 1321,
1358, 1361, 1369, 1397, 1479.
Thigmomorphogenesis 140, 141, 142, 143, 144.
Tissue culture: 51,75, 75a, 87, 180, 181,242,360,448,449,503,569,570,676,690,
729b, 734, 735, 736, 737, 745, 750, 755, 784, 800, 806, 905, 927, 938,
985, 1043a, 1054, 1129, 1130, 1131, 1159, 1252, 1327, 1328, 1360, 1406,
1407, 1416, 1445, 1447, 1481, 1483.
Tuberization : 338, 433, 435, 447.
Uptake in animal tissues: 243, 314, 526, 695, 717, 726, 1117, 1266.
Vacuoles: 124, 191,251,265,467,486,514,951,993,994, 1052, 1053, 1480.
Virus: 29,68, 71, 80, 81, 89,99, 109, 178, 198,420,773, 1221, 1222, 1267, 1299,
1341, 1366a, 1394, 1395, 1400, 1430, 1450, 1451.
Wall: 72, 109, 115, 144, 161, 192, 193,223,261,264,284,357,391,414,415, 423a.
467,485, 488a, 489,514,521,550,604,725,769,801.804.805. 828a,
849,850,870,951,952,993, 1044, 1053, 1078, 1109, 1110, 1271, 1283,
1284, 1434, 1435, 1436, 1436a, 1478, 1479, 1480.
Water potential : 274.
Water stress: 212, 275, 978.
Wound : 76, 77, 78, 79, 108, 109, 110, Ill, 113, 114, 115, 116,127, 129, 322. 498,
588,753,754,766,844,978, 1099, 1144, 1314, 1326.
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