Protein Nutrition (David Bender)

computing
Chapter 9
Introduction to Nutrition and Metabolism, 3rd edition

David A Bender
Taylor & Francis Ltd, London 2002
Chapter 9: Protein Nutrition and Metabolism

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Approximate body composition
computing
Approximate
water body composition
64%
essential fat
3%
storage fat
minerals 12%
protein
6%
15%
water
54%
essential fat
9%
storage fat
minerals 19%
5% protein
13%
dietary protein computing
80 gOverview of protein metabolism
body protein
enzymes (~ 10 kg)
intestinal cells
mucus
70 g
amino acids
amino acids
and dipeptides
urine
(70 g)
metabolites
faecal loss
(10 g)
Nitrogen balance
computing
The difference between:
Nitrogen balance
intake of nitrogenous compounds (mainly protein)
and excretion of nitrogenous metabolites
dietary protein
80 g
enzymes body protein
intestinal cells (~ 10 kg)
mucus
70 g
amino acids
amino acids
and dipeptides
urine
(70 g)
faecal loss metabolites
(10 g)
Nitrogen balance
computing
Nitrogen balance
INTAKE - equilibrium
= EXCRETION
N balance or equilibrium
normal state in an adult
no change in body protein content
dietary protein
80 g
mucus
70 g
amino acids
amino acids
and dipeptides
urine
(70 g)
(10 g)
Nitrogen balance
computing
Positive
INTAKEnitrogen balance
> EXCRETION
positive N balance
increase in body protein content
normal state in growth, pregnancy and recovery from loss
dietary protein
80 g
mucus
70 g
amino acids
amino acids
and dipeptides
urine
(70 g)
(10 g)
Nitrogen balance
computing
Negative
INTAKE nitrogen balance
< EXCRETION
negative N balance
decrease in body protein content
never normal; indicates illness, trauma or inadequate intake
dietary protein
80 g
mucus
70 g
amino acids
amino acids
and dipeptides
urine
(70 g)
(10 g)
Dynamic equilibrium:
the constant turnover of tissue components computing
Dynamic equilibrium - 1
Plus ça change, plus c’est la même chose
“Now here, you see” [saidDynamic
the Red Queen to Alice]- 2
equilibrium
“it takes all the running you can do to keep in the same place”
Lewis Carroll, Through the Looking Glass
Protein synthesis is energy expensive

minimal estimate: 4 mol ATP/GTP per peptide bond 2.80 kJ /g
allowing for ATP cost of transporting amino acids 3.59 kJ /g
allowing for ATP cost of synthesising mRNA 4.19 kJ /g
protein turnover in the fed and fasting states computing
Protein turnover in the fed and fasting states - 1
mmol /hour
synthesis catabolism
fed 8.8 8.1
fasting 6.4 7.85
In the fasting state amino acids from protein breakdown are being used
for gluconeogenesis and as metabolic fuel
In the fed state there is an ample energy supply for protein synthesis

protein turnover in the fed and fasting states computing
Protein turnover in the fed and fasting states - 2
energy turnover % energy

meal
expenditure g / hour expenditure
fasting - 1.95 8.7 %
high carbohydrate + 5.7 % 3.04 11.7 %
high protein + 9.6 % 6.47 19.8 %

Dynamic equilibrium - 3
All parts of the body of man

experience an intimate movement
that serves both
to expel those molecules that can or ought
no longer to compose the body,
and replace them with new ones
Magendie, 1829
mechanisms involved in protein catabolism computing
Mechanisms involved in protein catabolism - 1
lysosomal cathepsins
 broad range of specificities, complete hydrolysis of:
 proteins entering cell by phagocytosis
 proteins with the lysosomal targetting sequence
 Lys-Phe-Glu-Arg-Gly (KFERQ)
calpain-calstatin system
 calpain is a calcium-activated cysteine protease
 broad specificity for hydrophoibic amino acids
 has a calmodulin-like regulatory subunit
 inhibited by calstatin
mechanisms involved in protein catabolism computing
Mechanisms involved in protein catabolism - 2
ubiquitin-proteasome ATP-dependent system
 ubiquitin
 8.5k peptide
 forms peptide bond to e-amino group of lysine in target
protein (ATP-dependent)
 proteasome
 700k multi-enzyme complex
 (1% total soluble protein of cells)
 5 types of subunit with specificity for hydrophobic,
basic and acidic amino acid esters
 regulated by assembly of multi-enzyme complex
Dynamic
Schoenheimer (1946) equilibrium – Schoenheimer
fed rats 15N labelled amino acids
experiment
% recovery of label after feeding
[15N] leucine [15N]glycine
urine 2.2 2.6
faeces 27.4 40.8
carcase non-protein N 8.2 11.1
carcase protein 56.5 44.3
total 94.3 98.8
determination of half-lives of individual proteins computing
ornithine decarboxylase 11 min
Determination of half-lives of individual proteins
lipoprotein lipase 1h
tyrosine transaminase 1.5 h
label in protein
phosphoenolpyruvate 2h maximum label
carboxykinase
tryptophan oxygenase 2h
HMG CoA reductase 3h
glucokinase 12 h
alanine transaminase 0.7 – 1 d
serum albumin 3.5 d
arginase 4–5d
lactate dehydrogenase 16 d half life
adult collagen 300 d
infant collagen 1 – 2 d & 150 d time
Nitrogen balance – determination of protein requirements
computing
Nitrogen balance –INTAKE = EXCRETION
determination of protein requirements - 1
N balance or equilibrium
normal state in an adult
no change in body protein content
INTAKE < EXCRETION
negative N balance
decrease in body protein content
never normal; indicates illness, trauma or inadequate intake
INTAKE > EXCRETION
positive N balance
increase in body protein content
normal state in growth, pregnancy and recovery from loss
Nitrogen balance – determination of protein requirements
computing
Nitrogen balance – determination of protein requirements - 2
400
300
200
100
-100
-200
-300
-400
-500
80 0 30 40 100 100 50
daily protein intake (g)
Experimental basis of estimates of protein requirements
computing
Experimental
no of studies basis of estimatesprotein
duration of protein requirements
n
9 short-term single protein sources 93
8 short-term typical mixed diets 73
6 24 – 89 d 5 egg, 1 milk 34
short-term studies – average requirement for N balance = 0.63 g /kg bw
long-term studies – average requirement for N balance = 0.58 g /kg bw
Average requirement = 0.6 g protein /kg body weight

coefficient of variation = 12.5%
safe and adequate level of intake = 0.75 g /kg bw (UK average = 1.2)
safe and adequate level of intake = 7.5% of energy (UK average = 15%)
Protein deficiency is unlikely in an adult
Safe and adequate protein intake is 7.5 % of energy intake computing
If you can eat enough of most
Protein “starchy”
deficiency staples toinmeet
is unlikely energy needs
an adult
you will meet your protein requirements
cassava
yam
rice
barley
potato
rye
oatmeal
maize
pasta
wheat
0 3 6 9 12 15 18
protein, % energy
Essential and non-essential amino acids
computing
Essential and non-essential amino acids - 1
essential amino acids

 those that cannot be synthesized in the body
 but must be provided in the diet to maintain N balance
non-essential amino acids

 those that can be synthesized in the body
 from (common) metabolic intermediates
 and therefore can be synthesized (by transamination)
 as long as there is adequate total fixed N
Essential and non-essential amino acids
computing
Essential and non-essential amino acids - 2
essential
essential non-essential semi-essential
precursor
histidine alanine
isoleucine aspartic acid asparagine
leucine glutamic acid glutamine
lysine arginine
methionine cysteine glycine
phenylalanine tyrosine proline
threonine serine
tryptophan
valine
Semi-essential amino acids
computing
Semi-essential amino acids
Demand may outstrip synthetic capacity
under conditions of metabolic stress or trauma
semi-essential
 glutamine – in surgical trauma and sepsis

asparagine
 arginine – at times of high protein intake
glutamine
 arginine – at times of high growth
arginine
 glycine – with high intakes of some xenobiotics
glycine
 (excreted as glycine conjugates)
proline
 proline – in severe trauma
serine
 (requirement for collagen synthesis)
Indices of protein quality
computing
Indices of protein quality
Biological Value (BV)
• the proportion of absorbed protein retained in the body.
Net Protein Utilization (NPU)
• the proportion of dietary protein that is retained in the body (i.e. it
takes account of the digestibility of the protein).
Protein Efficiency Ratio (PER)
• the gain in weight of growing animals per gram of protein eaten.
Relative Protein Value (RPV)
• the ability of a test protein, fed at various levels of intake, to support
nitrogen balance, compared with a standard protein.
Chemical Score
• based on chemical analysis of the protein; it is the amount of the
limiting amino acid compared with the amount of the same amino acid
in egg protein (which is completely useable for tissue protein
synthesis).
Protein Score (or amino acid score)
• uses a reference pattern of amino acid requirements as the standard.
Sources of protein in the average British diet
computing
Sources of protein in the average British diet
other fruit and

fish eggs
vegetables
6% 4%
6%
meat
potatoes
38%
4%
milk
18%
other cereals bread

9% 15%
Protein loss over 10 days in response to trauma
computing
Protein loss over 10 days in response to trauma
tissue loss blood loss catabolism total
fracture of femur - 200 g 700 g 900 g
muscle wound 500 – 750 g 150 – 400 g 750 g 1350 – 1900 g
35% burn 500 g 150 – 400 g 750 g 1400 – 1650 g
gastrectomy 20 – 180 g 20 – 100 g 625 – 750 g 645 – 850 g
typhoid fever - - 675 g 685 g
The catabolic loss may be 6 – 7 % of total body protein over 10 days
Why is there protein loss in response to trauma ?
computing
Why is there protein loss in response to trauma ?
In response to trauma, acute phase proteins are synthesized
they are disproportionately rich in threonine and cysteine
This depletes tissue pools of these two essential amino acids

leaving an unbalanced amino acid mixture
that cannot be used for protein synthesis
These surplus amino acids are used as metabolic fuel
Why does an adult require so much protein ?
computing
Why does an adult require so much protein ? - 1
Mucus secreted in the gut
is disproportionately rich in threonine and cysteine
(as much as 60% of threonine requirement is for mucus synthesis)

computing
Why does an adult require so much protein ? - 2
Cortisol induces gluconeogenesis and breakdown of muscle protein
It acts on the liver, not on muscle
It induces tryptophan dioxygenase and tyrosine transaminase

computing
Several of the
Whyenzymes of amino
does an acid catabolism
adult require so much have high values
protein ? - 3 of Km
so their activity increases sharply
as the concentration of substrate increases in the fed state
aminoacyl tRNA synthetases Km = 1 – 50 µmol /L
lysine-ketoglutarate reductase Km = 18 mmol /L
phenylalanine hydroxylase Km = 660 µmol /L
branched chain aminotransferase Km = 4 mmol /L
fasting liver amino acid concentrations 30 – 50 µmol /L
There is irreversible loss of these amino acids as the concentrations rise

above that at which aminoacyl tRNA synthetases are saturated
The structure of DNA O
thymine computing
NH2 CH3
adenine HN
3' end
5' end
N The
N
structure of DNA -
OH1 free 3' hydroxyl group
free 5' hydroxyl group N
N deoxy-
HO CH2 N ribose
O
O O CH2 O
NH2 guanine
HO P O
cytosine N
O HN O
N
O P OH N
H2N N
O CH2 N O
O
O CH2 O
NH2
O cytosine HO P O
guanine
O N N O
NH
O P OH
N O N
O CH2 O N NH2
NH2 O CH2 O
O adenine
thymine HO P O
N
O H3C N
NH O
O P OH N
N
O CH2 N O
O
deoxy- O H C OH
ribose 2
5' end
free 5' hydroxyl group
3' end OH
The structure of DNA
O
thymine
computing
NH2 CH3
adenine HN
5' end
N
N The structure of DNA - 2
3' end
OH free 3' hydroxyl group
free 5' hydroxyl group N
N deoxy-
HO CH2 N ribose
O
O O CH2 O
NH2 guanine
HO P O
cytosine N
O HN O
N
O P OH N
H2N N
O CH2 N O
O
O CH2 O
NH2
O cytosine HO P O
guanine
O N N O
NH
O P OH
N O N
O CH2 O N NH2
NH2 O CH2 O
O adenine
thymine HO P O
N
O H3C N
NH O
O P OH N
N
O CH2 N O
O
deoxy- O H C OH
ribose 2
5' end
3' end OH
The genetic code
computing
first U The
C genetic code
A G third
Phe Ser Tyr Cys U
Phe Ser Tyr Cys C
U
Leu Ser STOP STOP A
Leu Ser STOP Trp G
Leu Pro His Arg U
Leu Pro His Arg C
C
Leu Pro Gln Arg A
Leu Pro Gln Arg G
Ile Thr Asn Ser U
Ile Thr Asn Ser C
A
Ile Thr Lys Arg A
Met Thr Lys Arg G
Val Ala Asp Gly U
Val Ala Asp Gly C
G
Val Ala Glu Gly A
Val Ala Glu Gly G
Protein synthesis - initiation
computing
Protein synthesis - initiation
P
P A
P
computing
Protein synthesis
P
P A
P
computing
P AP
computing
P AP
computing
P
P A
P
Termination
computing
Protein synthesis - termination
P A
Amino acid metabolism – deamination of amino acids
computing
D- and L-amino acidacid
D- and L-amino oxidases
oxidases
NH4+
R R
HC NH3+ C O
COO- COO-
O2
H2O2
amino acid keto-acid
(oxo-acid)
computing
Glycine oxidase
glycine oxidase
NH4+
H2 H2
C NH3+ C O
COO -
O2 COO-
H2O2
glycine glyoxylate
computing
glutamateGlutamate
dehydrogenase
dehydrogenase
COO- COO-
NH4+
CH2 CH2
CH2 CH2
HC NH3+ NAD+ C O
NADH
COO- COO-
glutamate ketoglutarate
(oxo-glutarate)
computing
Serine deaminase
serine deaminase
NH4+
CH2OH CH3
HC + C O
NH3
COO- COO-
serine pyruvate
Amino acid metabolism – transamination
computing
H
Amino acid metabolism – transamination 1
R1 C COO- R2 C COO-
NH3+ O
substrate amino acid substrate keto-acid
amino donor amino acceptor
R1 C COO- R2 C COO-
O NH3+
product keto-acid product amino acid
Amino acid metabolism – transamination
computing
Amino acid metabolism – transamination 2
OH H C O
H O P O CH2 OH H
R1 C COO- R2 C COO-
OH
NH3+ N CH3 NH3+
pyridoxal phosphate product amino acid
substrate amino acid
amino donor
OH CH2 NH2
R1 C COO- O P O CH2 OH R2 C COO-
O OH O
product keto-acid N CH3 substrate keto-acid

pyridoxamine phosphate amino acceptor
Transamination of amino acids to common intermediates
computing
alanine
Transamination of amino+
pyruvate
NH 3 acids to common intermediates
H3 C C O
H 3 C CH
-
CO O
- CO O
+
aspartic acid
-
NH 3 oxaloacetate
-
OOC CH 2 CH OOC CH 2 C O
- -
CO O CO O
glutamic acid NH 3
+ a-ketoglutarate
-
- OOC CH 2 CH 2 C O
OOC CH 2 CH 2 CH
-
- CO O
CO O
+
glycine NH 3 glyoxalate
HC H HC O
- -
CO O CO O
Amino acid metabolism – transamination + deamination
computing
COO-
Amino acid metabolism – transamination + deamination - 1
CH2
R
CH2
HC NH3+ NH4+
C O
COO- NADH
amino acid COO-
glutamate
transaminase ketoglutarate dehydrogenase
R COO - NAD+
C O CH2
COO- CH2
keto-acid HC NH3+
glutamate
COO-
Amino acid metabolism – transamination + deamination
computing
Amino acid metabolism – transamination + deamination - 2
R
HC O
HC NH3+ NH4+
COO-
COO- glyoxylate H2O2
amino acid
glycine
transaminase oxidase
H2C NH3+ O2
R
COO-
C O glycine
COO-
keto-acid
Ammonia metabolism – glutamate and glutamine synthesis
computing
Glutamate and glutamine synthesis
NH4+
glutamine synthetase
COO- COO- CONH2

NH4+ glutamate
CH2 CH2 CH2
dehydrogenase
ATP CH2
CH2 CH2
ADP, Pi
C O HC NH3+ HC NH3+
NADH COO- COO-
COO-
NAD+ glutamine
ketoglutarate glutamate H2O
NH4+ glutaminase
Glutamine synthetase
computing
Glutamine synthetase
ADP, Pi
COOH NH4+ ATP CONH2
CH2 CH2
CH2 overall reaction CH2
CH NH3+ CH NH3+
COO- COO-
glutamate OH glutamine
O C O P O
CH2 OH
ATP H3PO4
CH2
ADP CH NH3+ NH4+
COO-
-glutamyl phosphate
Excretion of nitrogenous waste
computing
Small aquatic organisms can excrete NH + into
Excretion of nitrogenous waste - 1 4
a large volume of water outside
fish excrete about 60% of N waste as NH4+

and the remainder as trimethylamine oxide
Terrestrial animals must produce a less toxic N metabolite to excrete
Excretion of nitrogenous waste
computing
Excretion of nitrogenous waste - 2 NH2
If water balance or weight is not a problem
then urea is the common product; it is readily soluble O C
ureotelic animals
NH2
If water balance is a problem (eg little water is available in the egg)

then uric acid is a common product
it has low solubility and crystallizes readily
birds and most insects are uricotelic

they excrete uric acid
arachnids and bats are purinotelic

they excrete mainly guanine
computing
Excretion of nitrogenous waste - 3
Tadpoles are aquatic – they excrete mainly NH4+
As they undergo metamorphosis

their N metabolism changes
adult frogs are largely terrestrial
and excrete urea
The Xenopus toad is largely aquatic

and excretes 70 – 80% of its N waste as NH4+
if it is removed from water it can form mainly urea
Urea synthesis – a cyclic biosynthetic pathway
The product is built up on a carrier molecule computing
that is unchanged
Urea synthesis –a
at the end of the cyclebiosynthetic
cyclic add pathway
add


add-on-a-bit
  on-a
add-on-a-bit
add-on-a add-on-a


bit
Urea synthesis
glutamine adenosine monophosphate
computing
glutaminase Synthesisadenosine
of carbamyl
deaminase phosphate
NH4+
glutamate inosine monophosphate
2 x ATP CO2 1 x N in urea comes from ammonia

the other from aspartate
2 x ADP
H3PO4
Carbamyl phosphate synthetase I
NH2 OH
has an absolute requirement for
O C O P O N-acetyl glutamate for activity
carbamyl OH
phosphate
N-acetyl glutamate is the precursor
carbamyl phosphate synthetase I for synthesis of arginine
mitochondrial enzyme
NH4+
CO2 2 ATP
carbamyl phosphate synthetase
computing
Urea synthesis NH2 OH
2 ADP, Pi
O C O P O NH2
carbamyl
OH C O
phosphate
NH3+ NH
CH2 Pi CH2
CH2 CH2
ornithine
CH2 CH2
carbamyltransferase
HC NH3+ HC NH3+ COO-
COO- COO- CH2

urea ornithine +H N
citrulline 3 CH
NH2
COO-
O C ATP aspartate
NH2 arginase argininosuccinate
synthetase
H2O
AMP, PPi COO-
CH2
H
HN C NH2 HN C N CH
NH NH COO- keto-acids
CH2 argininosuccinase CH2
transaminases
CH2 CH2 amino acids
CH2 CH2
HC NH3+ COO- HC NH3+
COO- CH COO-
arginine argininosuccinate
CH
fumarate
COO-
H2O COO- malate COO-

CH2 dehydrogenase CH2
fumarase
CHOH C O
COO- NAD+ NADH COO-
malate oxaloacetate
NH2 OH
O C O P O NH2
carbamyl
OH C O
computing
phosphate
Urea synthesis NH3+

CH2 Pi
NH
CH2
CH2 CH2
ornithine
CH2 CH2
carbamyltransferase
HC NH3+ HC NH3+ COO-
COO- COO- CH2

urea ornithine +H N
citrulline 3 CH
NH2
COO-
O C ATP aspartate
NH2 arginase argininosuccinate
synthetase
H2O
AMP, PPi COO-
CH2
H
HN C NH2 HN C N CH
NH NH COO-
CH2 CH2
CH2 CH2
COO- CH COO-
CH
fumarate
COO-
NH2 OH
computing
O C Ocarbamyltransferase
Ornithine P O NH2
carbamyl
OH C O
phosphate
NH3+ NH
CH2 Pi CH2
CH2 CH2
ornithine
CH2 CH2
carbamyltransferase
HC NH3+ HC NH3+
COO- COO-
ornithine citrulline
NH2
C O computing
NH
Argininosuccinate synthetase
CH 2
citrulline
CH2
COO-
CH2
CH2
HC NH3+
+ CH
H3N
COO-
COO-
ATP aspartate
argininosuccinate
synthetase
AMP, PPi COO-
CH2
H
HN C N CH
NH COO-
CH2
CH2
CH2 argininosuccinate
HC NH3+
COO-
computing
COO-
Argininosuccinase
CH2
H
HN C NH2 HN C N CH
NH NH COO-
CH2 CH2
CH2 CH2
HC NH3+ COO - HC NH3+
COO- CH COO-
CH
fumarate
COO-
NH3+
CH2 computing
CH2
ornithine Arginase
CH2
HC NH3+
urea
COO-
NH2
O C
NH2 arginase
H2O
HN C NH2
NH
CH2
CH2
CH2 arginine
HC NH3+
COO-
COO-
CH2
+
computing
citrulline H3N CH
Urea synthesis
ATP
COO-
aspartate
argininosuccinate
synthetase
AMP, PPi COO-
CH2
H
HN C NH2 HN C N CH
NH NH COO- keto-acids
transaminases
CH2 CH2 amino acids
CH2 CH2
COO- CH COO-
CH
fumarate
COO-
H2O COO- malate COO-

CH2 dehydrogenase CH2
fumarase
CHOH C O
COO- NAD+ NADH COO-
malate oxaloacetate
Urea synthesis from ammonium in isolated hepatocytes
computing
Urea synthesis from ammonium in isolated hepatocytes
urea formed
ammonium added
Urea synthesis – the effect of adding arginine
computing
Urea synthesis
urea formed
– the effect of adding arginine

Arg 0
Arg 2.5
Arg 5
Arg 10
ammonium added
Arg 0 Arg 2.5 mM Arg 5 mM Arg 10 mM

urea NH4+ 0 0 + 2.6 + 5.2 + 10.2
urea NH4+ 250 mM + 5.9 + 26.0 + 45.7 + 87.1
NH4+ NH4+ 0 - 5.8 - 23.3 - 41.0 - 75.2
Urea synthesis – the effect of adding ornithine
computing
Urea synthesis
urea formed
– the effect of adding ornithine

Orn 0
Orn 2.5
Orn 5
Orn 10
ammonium added
Orn 0 Orn 2.5 mM Orn 5 mM Orn 10 mM

urea NH4+ 0 0 0 0 0
urea NH4+ 250 mM + 5.8 + 21.4 + 36.8 + 64.9
NH4+ NH4+ 0 - 5.8 - 21.5 - 35.9 - 65.1
Urea synthesis – the effect of adding citrulline
computing
urea formed
Urea synthesis – the effect of adding citrulline

Cit 0
Cit 2.5
Cit 5
Cit 10
ammonium added
Cit 0 Cit 2.5 mM Cit 5 mM Cit 10 mM

urea NH4+ 0 0 + 2.6 + 5.2 + 10.2
urea NH4+ 250 mM + 5.9 + 26.0 + 45.7 + 87.1
NH4+ NH4+ 0 - 5.8 - 23.3 - 41.0 - 75.2
O
HN
N
computing
keto-acids
COO-
amino acids Adenosine
COO
N
-
N
deaminase
ribose phosphate
CH2 CH2 inosine monophosphate
C O transaminasesHC NH3+ GTP
adenylosuccinate
COO- COO- synthetase
oxaloacetate aspartate
GDP, Pi
-OOC CH2 CH COO-
NH NH4+
NADH adenosine
N deaminase
malate dehydrogenase N
H2O
NAD+ N N
ribose phosphate
COO- H2O COO- adenylosuccinate

CH2 CH adenylosuccinase
CHOH fumarase CH NH2

COO- COO-
malate fumarate N
N
N N
adenosine monophosphate ribose phosphate
computing
End
Introduction to Nutrition and Metabolism, 3rd edition

David A Bender
Taylor & Francis Ltd, London 2002
Chapter 9: Protein Nutrition and Metabolism

End of presentation
The urea synthesis and nitrogen balance simulations on the CD
accompany this Chapter
Presentation copyright © 2002 David A Bender and some images copyright © 2002 Taylor & Francis Ltd

Protein Nutrition (David Bender)

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Introduction to Nutrition and Metabolism, 3rd edition

Chapter 9: Protein Nutrition and Metabolism

Plus ça change, plus c’est la même chose

Protein synthesis is energy expensive

Protein synthesis is energy expensive

energy turnover % energy

fasting - 1.95 8.7 %

high carbohydrate + 5.7 % 3.04 11.7 %

high protein + 9.6 % 6.47 19.8 %

Protein synthesis is energy expensive

All parts of the body of man

[15N] leucine [15N]glycine

urine 2.2 2.6

faeces 27.4 40.8

carcase non-protein N 8.2 11.1

carcase protein 56.5 44.3

total 94.3 98.8

daily protein intake (g)

9 short-term single protein sources 93

8 short-term typical mixed diets 73

short-term studies – average requirement for N balance = 0.63 g /kg bw

long-term studies – average requirement for N balance = 0.58 g /kg bw

Average requirement = 0.6 g protein /kg body weight

essential amino acids

non-essential amino acids

 glutamine – in surgical trauma and sepsis

other fruit and

other cereals bread

fracture of femur - 200 g 700 g 900 g

muscle wound 500 – 750 g 150 – 400 g 750 g 1350 – 1900 g

35% burn 500 g 150 – 400 g 750 g 1400 – 1650 g

gastrectomy 20 – 180 g 20 – 100 g 625 – 750 g 645 – 850 g

typhoid fever - - 675 g 685 g

The catabolic loss may be 6 – 7 % of total body protein over 10 days

This depletes tissue pools of these two essential amino acids

These surplus amino acids are used as metabolic fuel

This depletes tissue pools of these two essential amino acids

These surplus amino acids are used as metabolic fuel

It induces tryptophan dioxygenase and tyrosine transaminase

This depletes tissue pools of these two essential amino acids

These surplus amino acids are used as metabolic fuel

aminoacyl tRNA synthetases Km = 1 – 50 µmol /L

lysine-ketoglutarate reductase Km = 18 mmol /L

phenylalanine hydroxylase Km = 660 µmol /L

branched chain aminotransferase Km = 4 mmol /L

fasting liver amino acid concentrations 30 – 50 µmol /L

There is irreversible loss of these amino acids as the concentrations rise

R1 C COO- O P O CH2 OH R2 C COO-

product keto-acid N CH3 substrate keto-acid

COO- COO- CONH2

ADP CH NH3+ NH4+

fish excrete about 60% of N waste as NH4+

Terrestrial animals must produce a less toxic N metabolite to excrete

If water balance is a problem (eg little water is available in the egg)

birds and most insects are uricotelic

arachnids and bats are purinotelic

Tadpoles are aquatic – they excrete mainly NH4+

As they undergo metamorphosis

The Xenopus toad is largely aquatic

2 x ATP CO2 1 x N in urea comes from ammonia

COO- COO- CH2

H2O COO- malate COO-