8 - Biochem (BusySPR 2016 SBAs)

This Copy is for Dr.
Mohamed ElHodiby
NUCLEOTIDES & NUCLEIC ACIDS
Question 1 With respect to the structure of nucleic acids

A Purine bases include guanine and thymine B Purine bases include thymine and cytosine
C Pyrimidine bases include ribose and deoxyribose D Pyrimidine bases include thymine and cytosine
E Uracil is both a purine and a pyrimidine base
A(Correct answer: D)
Explanation
NUCLEOTIDES
· Base - purine (guanine -G and adenine -A) or pyrimidine (thymine -T, cytosine -C and
uracil -U) *
· Pentose (5-carbon) sugar - ribose (RNA) or deoxyribose (DNA) Phosphate *
· Uracil is found only in RNA and replaces thymine *
· Nucleotides are linked by 3-5-phosphodiester bonds to form nucleic acids. The 3-end of
the chain has a free OH group while the 5- end has a phosphate group. During synthesis,
nucleotides are added to the 3- end

A DNA: ribose sugar, no uracil and no purine bases B RNA: ribose sugar, uracil, purine and pyrimidine bases
DNA: purine and pyrimidine bases, uracil, no ribose RNA: 6-carbon sugar, uracil, purine and pyrimidine
C D
sugar bases
DNA: 6 carbon sugars, purine and pyrimidine bases,
E
no uracil
A(Correct answer: B)
Explanation
Same as of Question 1
Question 3 Nucleic acids are formed from

A Nucleotides linked by 3-5-phosphodiester bonds B Ribose linked to deoxyribose by hydrogen bonds
Purine bases linked to pyrimidine bases by hydrogen
C Nucleotides linked to ribose or deoxyribose D
bonds
Purine bases linked to ribose sugars by 3-5-
E
phosphodiester bonds
A(Correct answer: A)
Explanation
This Copy is for Dr. Mohamed ElHodiby

Question 4 Which one is not a recognized family of histones

A H1 / H5 B H2A
C H2B D H2C
E H4
Explanation
· The DNA in chromosomes is associated with several proteins, of which histones are the
most abundant
· HISTONES are highly basic, positively charged arginine / lysine rich proteins which
interact with the negatively charged phosphate groups on DNA
· Five major families of histones exist: H1/H5, H2A, H2B, H3 and H4.
· Histones H2A, H2B, H3 and H4 are known as the core histones, while histones H1 and
H5 are known as the linker histones
· DNA is wound around a histone octamer made up of two molecules of H2A, H2B,H3 &
H4 to form beads called nucleosomes
· Nucleosomes are joined by threads of double stranded (linker) DNA which is bound to
histone H1 giving a -beads on a string- appearance
· The ratio of DNA to histones in chromosomes on a weight basis is ~ 1:1
· Nucleosomes are organised into 30nm fibres which are then attached to a central protein
scaffolding a series of radial loops
Question 5 To form nucleosomes, DNA is wrapped around

A Histone octamers B Histone dimers
C Histone tetramers D Chromatin
E Spindle fibres
Explanation
Question 6 Histones are integral to the structure of the chromosome. Which one is the linker histone(s)

A H2A B H2B and H3
C H3 and H4 D H1 and H3
E H1 and H5
A(Correct answer: E)
Explanation

Question 7 With respect to the structure of DNA and chromosomes, nucleosomes are joined by

A Single-stranded linker DNA B Double-stranded RNA
C Double-stranded linker DNA D 3-5-phosphodiester bonds
E hydrogen bonds
A(Correct answer: C)
Explanation
Question 8 With respect to the structure of DNA and chromosomes, nucleosomes are joined by

A Double-stranded DNA bound to histone H1 B Double-stranded DNA bound to histone H2
C Double-stranded DNA bound to histone H4 D Double-stranded DNA bound to histone H2A
E Single-stranded DNA bound to histone H4
Explanation
Question 9 In a chromosome, the ratio of DNA to histones on a weight basis is

A 10 : 1 B 5:1
C 2:1 D 1:1
E 0.1 : 1
Explanation
Question 10 Messenger RNA (mRNA)

A Is synthesized during translation B Is monocistronic
C Has size measured in kilo Daltons D Is synthesized by DNA polymerase
E Does not contain exons

Explanation
MESSENGER RNA
· Single stranded and monocistronic (one mRNA molecule only codes for one protein).
Synthesized from DNA in the process of transcription by RNA polymerase. Mature mRNA does
not contain introns and exons - introns are removed during splicing before transport into the
cytoplasm *
· The size of RNA molecules is quoted in Svedberg units (S)
· Sequence is written in 5- to 3- direction. Has a 5- methylated cap followed by a leader
sequence then the start codon (AUG) followed by the translated region and the 3- poly-A tail *
· Relatively unstable and is broken down rapidly after transcription
· Uracil replaces Thymine in RNA and the sugar unit is RIBOSE *
· Detected by Northern blotting or by PCR
Question 11 Svedberg units

Are segments of DNA following digestion by
A B Are units of size for DNA
restriction enzymes
C Are units of size for mRNA D Are individual turns in the DNA double helix structure
E Are segments of non-coding DNA
Explanation
Question 12 Mature messenger RNA

A Contains introns and exons B Does not contain exons
C Does not contain introns or exons D Does not contain introns
E Can contain both introns and exons
Explanation

Question 13 In eukaryotic cells, ribosomes have 2 sub-units which are

A 10S and 40S B 20S and 40S
C 30S and 50S D 30S and 60S
E 40S and 60S
Explanation
RIBOSOMAL RNA
· Makes up 80% of total cellular RNA *

· Relatively stable due to its association with proteins
· Essential for protein synthesis *
· Has secondary structure with base-pairing within the molecule allowing the formation of
helical regions and hairpin loops
· Contains several modified nucleotides, especially 2-methylation on ribose
· RIBOSOMES: Eukaryotic ribosomes are 80S and dissociate into 40S and 60S subunits
· The 40S subunit has an 18S rRNA molecule and about 34 different proteins *
· The 60S subunit has 5S, 5.8S and 28S rRNA molecules and about 50 different proteins *
Question 14 With respect to the differences between mRNA and rRNA

A mRNA is more stable than rRNA B There is base-paring within mRNA but not rRNA
mRNA does not have a secondary structure while mRNA does not have a poly-A tail while rRNA has a
C D
rRNA has a secondary structure poly-A tail
E mRNA is 80S in size while rRNA is 40S or 60S
Explanation
Question 15 With respect to transfer RNA

There is a specific transfer RNA molecule for every Some amino acids are recognized by more than one
A B
protein specific tRNA
Some proteins are coded by more than one specific Some tRNA molecules recognize more than one amino
C D
tRNA acid
E tRNA does not have a secondary structure

Explanation
TRANSFER RNA
· Makes up 15% of total RNA
· Binds specific amino acids and carries them to the polyribosomes for protein synthesis
· There is a specific tRNA for each amino acid but some amino acids are recognised by
more than one specific tRNA and therefore have more than one codon *
· Has a clover-leaf secondary structure with an amino acid binding site at the 3- end and an
anticodon site on one of the clover leaves. The anticodon recognises the triplet codon on mRNA
*
Question 16 Which nucleic acid has a clover-leaf secondary structure?

A DNA B rRNA
C tRNA D mRNA
E tRNA bound to mRNA
Explanation
Question 17 Transcription

A Is the conversion of information in mRNA to proteins B Is the conversion of information in DNA to proteins
Is the transfer of mRNA from the nucleus to the
C Is the conversion of information in DNA to mRNA D
cytoplasm
E Is the movement of the tRNA along the mRNA chain
Explanation
TRANSCRIPTION
· Process by which the genetic information in DNA is converted to RNA. Occurs in the
nucleus *
· Catalysed by RNA polymerases *
· RNA polymerase I - synthesizes rRNA
· RNA polymerase II - synthesizes mRNA
· RNA polymerase III - synthesizes rRNA and tRNA
· Only the anti-sense DNA strand is transcribed. The mRNA molecule is synthesized in the
5- to 3- direction
· RNA polymerase does not have a nuclease activity and cannot remove any incorrect
bases. A primer is not required for RNA synthesis *

Question 18 Transcription is catalyzed by

A DNA polymerase B RNA polymerase
C DNA synthetase D RNA synthetase
E Restriction enzymes
Explanation
Question 19 Messenger RNA is synthesized by

A RNA polymerase I B RNA polymerase I & II
C RNA polymerase II D RNA polymerase II & III
E RNA polymerase III
Explanation
Question 20 Post-transcriptional mRNA processing includes

A Addition of exons B Removal of exons
C Addition of introns D Removal of introns
E Conversion of introns into exons
Explanation
RNA processing then occurs to produce mature mRNA ready for translation *
1) Addition of 5- methylated cap - protects the 5- end against ribonuclease degradation and
plays a role in the initiation of protein synthesis
2) Addition of 3- poly-A tail -cleavage and addition of 200-250 A residues - protects against
nuclease degradation and increases translational efficiency
3) SPLICING to remove introns: the coding regions of DNA (EXONS) are separated by non-
coding regions (INTRONS). After transcription, the introns are excised in SPLICEOSOMES. All
introns have a sequence which begins with 5-GU and ends with AG-3-. The introns are excised
and the exons joined. *
4) Alternative splicing occurs when one or more exons are excised together with the introns
in certain tissues. Non-coding regions are never present in mature mRNA
5) RNA editing - the mRNA sequence may be changed after synthesis and processing and
nucleotides may be substituted, added or deleted

Question 21 Introns have a sequence

A That begins with 5-GU B That ends in 5-GU
C That begins with 3-AG D That begins with 5-AG
E That ends with 3-GU
Explanation
Question 22 During the cell cycle, DNA synthesis occurs
A In the S and M phases B In the S, G1 and G2 phases

C In the M, G1 and G2 phases D In the S and G1 phases
E In the S phase
Explanation
DNA REPLICATION
• Occurs during the S phase of the cell cycle resulting in doubling of genetic material
• During the G2 phase, the cell is tetraploid. The G2 phase is followed by the M (mitosis)
phase when the genetic material is halved and diploid daughter cells are formed. The G1 phase
follows the M phase and some cells stop dividing and enter a G0 phase
Question 23 During DNA replication

The double helix is unwound at 20-80 sites forming
A The double helix is unwound by DNA ligase B
Okazaki fragments
C The leading strand is synthesized in Okazaki fragmentsD The action of DNA helicase produces 20-80 replicons
E DNA polymerase beta synthesizes the leading strand
Explanation
DNA replication
• DNA helix is unwound by DNA helicase at 20-80 sites forming replicons or replication
units *?
• There are 5 DNA polymerase enzymes which are responsible for replication:
• Polymerase - alpha synthesizes the lagging strand via Okazaki fragments
• Polymerase beta and epsilon repair DNA ?

• Polymerase delta synthesizes the leading strand ?
• Polymerase gamma replicates mitochondrial DNA ?
• Telomerase is a DNA polymerase with an integral RNA that acts as its own primer and
replicates DNA at the ends of chromosomes (telomeres) ?
• Replication is initiated by the synthesis of a primer sequence of RNA. Chain elongation
occurs in the 5' to 3' direction on the leading strand and in Okazaki fragments on the lagging
strand (discontinuous). The fragments are joined by DNA ligase ?
• Histones do not dissociate from DNA prior to replication. Histones are also synthesized
during the S phase and the old nucleosomes stay with the daughter DNA molecule containing
the leading strand while new nucleosomes assemble on the daughter molecule containing the
lagging strand. ?
• Rapidly dividing (malignant) cells are most sensitive to anti-metabolite chemotherapy
during the S phase of the cell cycle *?
Question 24 With respect to the action of DNA polymerases

DNA polymerase alpha – synthesizes the lagging
A B DNA polymerase alpha – repairs DNA
strand of DNA
DNA polymerase gamma – synthesizes the leading
C D DNA polymerase delta – produces Okazaki fragments
strand of DNA
E DNA polymerase beta – replicated DNA at telomeres
Explanation
Rapidly dividing (malignant) cells are most sensitive to anti-metabolite chemotherapy

Question 25
during which phase of the cell cycle?
A G0 Phase B G1 phase
C M phase D S phase
E G2 phase
Explanation
Rapidly dividing (malignant) cells are most sensitive to anti-metabolite chemotherapy during the
S phase of the cell cycle *?

The polymerase chain reaction is used to amplify DNA sequences. The DNA product is
Question 26
then identified using
A Western blotting B Northern blotting

C Restriction endonucleases D Light microscopy
E Fluorescent in-situ hybridization
Explanation
Options POLYMERASE CHAIN REACTION - PCR
• Enables the rapid amplification of DNA sequences in small biological samples *
• Used for pre-natal diagnosis and forensic medicine *
• Based on the use of DNA polymerases which function at high temperatures *
• Require the presence of DNA primers which flank the DNA sequence to be amplified and
deoxyribonucleotides
• Begins with the denaturation of DNA by heating to 90C *
• Primers anneal to the sequences to be amplified at 50C
• Extension of the primer sequence occurs at 70C
• The sequence is repeated usually over 30-35 cycles
• The DNA is separated by electrophoresis and the amplified sequences are visualised *
• Based on the primers used, the size of the PCR product can be predicted and this is used
in identification
• Further identification of PCR products requires sequencing to confirm their identity or use
of restriction endonucleases which should cut the sequence at a predicted point, with products
of predictable sizes *
The polymerase chain reaction has been used to amplify a specific DNA sequence. In
Question 27 order to identify the amplified DNA, it needs to be cut into fragments of specific sizes.
Which enzymes undertake this function?
A DNA ligase B DNA helicase

C DNA polymerases D Telomerases
E Restriction endonucleases
Explanation
RESTRICTION ENDONUCLEASES
• Enzymes which recognise specific DNA sequences and cut DNA at specific sites *
• Recognise palindromic sequences - sequences that are identical when read from left to
right and from right to left - AATTAA
• Cut DNA leaving 'blunt' ends - no bases sticking out, or 'sticky' ends with bases sticking
out, allowing complementary pairing with another chain
• May be used for the identification of PCR products as they cut at predictable sites, and
should produce fragments of predictable sizes if the identity of the PCR product is correct *

Question 28 With respect to techniques used to detect macromolecules

A Northern blotting – DNA B Southern blotting – DNA
C Western blotting – RNA D Eastern blotting – mRNA
E Western blotting – DNA
Explanation
DETECTION OF MACROMOLECULES
• Western blotting - protein
• Northern blotting - RNA
• Southern blotting – DNA
Question 29 Vectors are

A Fragments of DNA outside cells B Fragments of RNA outside cells
DNA species that can enter cells and replicate within
C DNA species that can replicate outside cells D
them
DNA species that can enter cells and inhibit DNA
E
replication
Explanation
VECTORS
• DNA species which can enter cells readily, remain stable and replicate within these cells
• Include plasmids and bacteriophages
• Plasmids are small circular DNA sequences which occur naturally in bacteria in which they
replicate independent of chromosomal DNA
• Plasmid entry into bacteria is facilitated by exposure of bacteria to an electric field (electroporation)
or treatment with CaCl2 and exposure to 40C heat. Plasmid infected cells are transformed and replicate
forming a clone
• Plasmids confer different phenotypic characteristics to bacteria, including antibiotic resistance
• Viruses that infect bacteria are Bacteriophages
Question 30 Plasmids

A Are viruses B Occur naturally in bacteria
C Integrate into bacterial DNA before replication D Are bacteria
E Infect viruses
Explanation

Question 31 Which amino acids are converted to cysteine in the human adult liver?

A Serine and valine B Arginine and lysine
C Glutamine and lysine D Histidine and proline
E Methionine and serine
Explanation
Classification according to side-chain *****
• Aliphatic - alanine, glycine, isoleucine, leucine, proline, valine
• Aromatic- phenylalanine, tryptophan , tyrosine
• Acidic- aspartic acid, glutamic acid
• Basic- arginine, histidine, lysine
• Hydroxylic- serine, threonine
• Sulphur-containing- cysteine, methionine, taurine
• Amidic (containing amide group)- asparagine, glutamine
Methionine + serine are converted to cysteine in the liver, a precursor for glutathione
synthesis.Cystathionase, is the enzyme that is necessary to convert cystathionine into cysteine, and is
present in humans post-natally *
Cystathionase is not present in human fetal liver or brain. *
Question 32 Which one is an essential amino acid in the fetus but not the adult?

A Arginine B Valine
C Cysteine D Methionine
E Phenylalanine
Explanation
Cysteine is not an essential amino acid in adults but is an essential amino acid for the human fetus, and
for prematurely born and full term infants for a short period after birth. *
· Cysteine concentration in maternal plasma is greater than or equal to that in fetal plasma
· Methionine is also a precursor for taurine synthesis

Proteins are synthesised from amino acids using the genetic code.
Question 33
Each codon is made up of
A 2 bases B 3 bases
C 4 bases D 3 or 4 bases
E 3 base pairs
Explanation
URIC ACID *****
· Produced from the breakdown of purine bases in the liver *
· Plasma concentration higher in males (202 - 406 microM) than in females (148 - 357 microM) *
· Weak acid with a pK of 5.8. At pHs below the pK, it exists predominately in a nonionized form
· The urate ion is more soluble than the nonionized molecule.
· Urate ions are about 5% protein bound.
· Urate is filtered at the glomerulus. *
· The renal tubule can reabsorb or secrete. Typically, net reabsorption occurs in infants and children
while net secretion occurs in adults *
· The kidneys excrete two-thirds of the uric acid produced daily; the remaining one-third is excreted in
the stool
· In early pregnancy uric acid levels fall by about one-third but rise to non-pregnant levels by term *
Question 34 In the human adult, uric acid levels

A Are higher in women than in men B Fall in early pregnancy
C Increase slightly in early pregnancy D Double by 12 weeks gestation
Are 50% lower in the term normal pregnancy
E
compared to outside pregnancy
Explanation
Causes of raised Plasma uric acid concentration *****
· Renal diseases with renal failureand prerenal renal failure (e.g. dehydration)
· Gout.
· Drugs - diuretics, pyrazinamide, ethambutol, nicotinic acid, and aspirin in low doses. *
· Excessive cell death - neoplasia, even before as well as following chemotherapy and radiotherapy,
especially lymphoma and leukemia; hemolytic anemia, resolving pneumonia and other inflammation;
polycythemia, myeloma, pernicious anemia, infectious mononucleosis, congestive heart failure, large
myocardial infarct. *
· Endocrine conditions: hypothyroidism, hypoparathyroidism, hyperparathyroidism,
pseudohypoparathyroidism; diabetes insipidus of nephrogenic type, Addison disease.
· Lead poisoning
· Hyperlipidaemia
· Acidosis: lactic acidosis, diabetic ketoacidosis, alcoholic ketosis.
· Pre-eclampsia *

· Dieting, weight loss, fasting or starvation. *
· Decreased urate clearance: cyclosporine-induced hyperuricemia.
Low uric acid concentration *****

· Drugs - allopurinol, corticosteroids and probenecid cause low uric. Massive doses of vitamin C are
uricosuric
· Poor dietary intake of purines and protein; tea, coffee.
· Renal tubular defects, Fanconi syndrome, late in Wilson disease
Question 35 Which one is not associated with raised plasma uric acid levels?

A Gout B Pre-renal renal failure
C Low dose aspirin D Diabetic keto-acidosis
E Corticosteroid therapy
Explanation
Question 36 With respect to renal handling of urea

A Urea is freely filtered at the glomerulus B Urea is secreted into the proximal tubule
Urea is transferred across the proximal tubule by Urea is actively absorbed by the distal loop of
C D
facilitated diffusion Henle
E 99% of filtered urea is actively reabsorbed
Explanation
Freely filtered at the renal glomerulus. *
· About 50% of the filtered urea is reabsorbed passively in the proximal tubule by a paracellular route
· Urea is secreted into the tubule fluid in the descending limb of the loop of Henle by carrier mediated
transport *
· Final urea excretion is dependent on the additional amount reabsorbed by carrier-mediated
transport in the medullary collecting ducts. This reabsorption increases at low urine flows and decreases
at high urine flows and is controlled by ADH. *

With respect to the renal handling of urea, carrier-mediated secretion of urea into
Question 37
the tubular fluid occurs in
A The glomerulus B The proximal convoluted tubule

C The collecting ducts D The renal pelvis
E The descending limb of the loop of Henle
Explanation
Question 38 With respect to renal excretion of urea, carrier-mediated reabsorption occurs in

C The descending limb of the loop of Henle D The medullary collecting ducts
E The renal pelvis
Explanation
Question 39 Urea reabsorption in the medullary collecting ducts
A Is independent of anti-diuretic hormone B Increases at low urine flow rates

C Increases at high urine flow rates D Decreases at low urine flow rates
E Occurs by passive diffusion
Explanation

Question 40 With respect to cholesterol metabolism, cholesterol is
A Mainly excreted by the kidneys B Mainly synthesised from triglycerides

C Mainly synthesised from phospholipids D Synthesised from acetyl CoA
E Mainly excreted as cholesterol phosphate
Explanation
CHOLESTEROL *****
· Component of cell membranes and precursor of steroid hormones and vitamin D *
· C27 compound, all derived from acetyl CoA. The acetate units are initially converted to C5 isoprene
units *
· Can be obtained from diet or synthesised in the liver *
· High levels of cholesterol and its metabolites reduce the activity of HMG coA reductase, the enzyme
catalysing the committed step in cholesterol synthesis
· Cholesterol is mainly excreted as bile salts and bile acids - glycocholate (glycine conjugate) or
taurocholate (taurine conjugate) *
Question 41 Simple triglycerides have
A Three identical fatty acid chains B Three glycerol molecules

C Unsaturated fatty acid chains D Saturated fatty acid chains
E Only one fatty acid chain
Explanation
TRIGLYCERIDES *****
· Three faty acid chains esterified to a glycerol backbone *
· Simple triglycerides have three identical fatty acids while mixed triglycerides have 2 or 3 different
fatty acids *
· Major dietary lipid in humans and major energy store
· Synthesised from glycerol-3-phosphate (glycolytic intermediate) and fatty acyl CoA
· Fatty acids removed from triglycerides by the action of lipase and the free fatty acids degraded by
beta-oxidation
· Glucagon, adrenaline and noradrenaline increase plasma free fatty acid concentration while insulin
has the opposite effect *
· May accumulate in the liver (fatty liver) *

Question 42 With respect to lipoproteins

A Chylomicrons are denser than HDL B VLDL carries triglycerides from cells to the liver
HDL caries phospholipids and cholesterol to the There is an association between high levels of
C D
liver HDL and atherosclerosis
High levels of LDL are known to protect against
E
atherosclerosis
Explanation
LIPOPROTEINS *****
· Globular particles consisting of a hydrophobic core and a hydrophilic surface. Contain triglycerides,
cholesterol, phospholipids, apoproteins
· Five different types
· With respect to density: Least dense: Chylomicron < VLDL < LDL < HDL most dense *
· Chylomicrons carry triglycerides from the intestines to the liver, skeletal muscle and adipose tissue.
· Very-low-density lipoproteins (VLDL) carry (newly synthesised) triglycerides from the liver to
adipose tissue.
· Intermediate-density lipoproteins (IDL) are intermediate between VLDL and LDL. They are not
usually detectable in the blood when fasting.
· Low-density lipoproteins (LDL) carry 3,000 to 6,000 fat molecules (phospholipids, cholesterol,
triglycerides, etc.) around the body. LDL particles are sometimes referred to as "bad" lipoprotein because
concentrations, dose related, correlate with atherosclerosis progression.
· High-density lipoproteins (HDL) collect fat molecules (phospholipids, cholesterol, triglycerides, etc.)
from the body's cells/tissues, and take it back to the liver. HDLs are sometimes referred to as "good"
lipoprotein because higher concentrations correlate with low rates of atherosclerosis progression and/or
regression
Question 43 With respect to the regulation of glycogen metabolism

A Adrenalin inhibits glycogenolysis B Adrenalin stimulates glycogen synthesis
Adrenalin stimulates the phosphorylation of
C D Adrenalin activates protein phosphatase I
phosphorylase b
Adrenaline stimulates the phosphorylation of
E
protein phosphatase I
Explanation
REGULATION OF GLYCOGEN METABOLISM *****
 Regulated by the phosphorylation and dephosphorylation of phosphorylase (glycogenolysis) and
glycogen synthase (glycogen synthesis)
 Phosphorylase exists as a phosphorylated active 'a' form and a dephosphorylated inactive 'b' form
 Glycogen synthase exists as a phosphorylated INACTIVE 'b' form and a dephosphorylated active 'a' form
 Phosphorylation / dephosphorylation is regulated by the activity of phosphorylase kinase and protein
phosphatase I

 GLUCAGON / ADRENALINE - stimulate the phosphorylation of inactive phosphorylase ′ b′, converting it
into active phosphorylase ′a′ and glycogenolysis is stimulated *
 Phosphorylation of glycogen synthase converts the active 'a' form to the inactive 'b' form and glycogen
synthesis is inhibited
 INSULIN - results in the phosphorylation and activation of protein phosphatase I *
 Phosphorylated and active phosphorylase 'a' is de-phophorylated and inactivated - glycogenolysis is
inhibited *
 Phosphorylated and inactive glycogen synthase 'b' is dephosphorylated and activated - glycogen
synthesis is activated *
 Calcium ions released during muscle contraction stimulate glycogenolysis. Skeletal muscle glycogen
cannot be converted into glucose. *
Question 44 Which molecule(s) can be metabolised by glycolysis?

A Glucose only B Glucose and fructose only
C Glucose and galactose only D Glucose and lactose only
E Glucose, fructose and galactose only
Explanation
GLYCOLYSIS *****
 Occurs in the cytoplasm and does not require oxygen. Principal energy generating mechanism in the
absence of oxygen of in cells such as RBC which do not have mitochondria *
 Initial reactions involve two phosphorylation steps: initially by hexokinase to form glucose-6-phosphate
(converted to fructose-6-phosphate by isomerase) and then to fructose 1,6 bisphosphate by
phosphofructokinase with the hydrolysis of ATP to ADP
 All reactions in the glycolysis pathway are reversible except those catalysed by hexokinase,
phosphofroctokinase and pyruvate kinase
 Glycolysis can be summarised by:
Glucose + 2Pi + 2ADP + 2NAD+ = 2pyruvate + 2H2O + 2ATP + 2NADH + 2H+ *

 Pyruvaye can be reduced to Lactate, converted to Acetyl CoA or Oxaloacetate
 Fructose and galactose can both be metabolised by glycolysis *
Question 45 The enzyme phosphofructokinase plays a key role in
A Gluconeogenesis B Glycolysis
C Glycogen synthesis D Glycogenolysis
E The Cori cycle
Explanation
REGULATION OF GLYCOLYSIS AND GLUCONEOGENESIS *****
 Unregulated glycolysis and gluconeogenesis would result in the futile consumption of ATP

 Glycolysis is inhibited when ATP and synthetic intermediates are in excess and gluconeogenesis inhibited
when ATP levels are low and ADP levels are high
 The main sites of regulation are at the reactions catalysed by phosphofructokinase (PFK - glycolysis) and
fructose 1,6 bisphosphatase (gluconeogenesis)
 AMP activates PFK (glycolysis and ATP synthesis) but inhibits fructose 1,6 bisphosphatase
 ATP inhibits PFK (glycolysis) and pyruvate kinase (glycolysis)
 Citrate (citric acid cycle) inhibits PFK (glycolysis) and stimulates fructose 1,6 bisphosphatase
 Glucagon released during starvation inhibits the synthesis of fructose 2,6 bisphosphate while insulin
stimulates its synthesis. Fructose 2,6 bisphosphate activates PFK (glycolysis) and inhibits fructose 1,6
bisphosphatase
 The amino acid alanine inhibits pyruvate kinase (glycolysis)
Question 46 Fatty acid synthesis occurs in

A The lysosomes B The cytoplasm
C The golgi apparatus D The smooth endoplasmic reticulum
E The rough endoplasmic reticulum
Explanation
FATTY ACID SYNTHESIS *****
 Takes place in the cytosol
 Mediated by a single polypeptide enzyme - fatty acid synthase with several enzymatic domains
 The committed step in the pathway is the conversion of acetyl CoA to malonyl CoA by acetyl CoA
carboxylase
 Occurs by the repetitive addition of two carbon units from malonyl CoA which has a three carbon unit,
with the release of CO2
ATP is consumed during fatty acid synthesis
Question 47 Which one inhibits the activity of hormone-sensitive lipase?

A Glucagon B Adrenaline
C ACTH D Noradrenaline
E Insulin
Explanation
BREAKDOWN OF TRIGLYCERIDES
 Occurs in the cytoplasm
 Mediated by hormone sensitive lipase which is activated by glucagon, adrenaline, noradrenaline and
ACTH through phosphorylation
 Insulin causes dephosphorylation and inactivation of hormone sensitive lipase
 Triglycerides are converted to one molecule of glycerol and three fatty acids
 Glycerol can enter glycolysis through phosphorylation to glycerol-3-phosphate

Question 48 Ketone bodies are produced when

The rate of fatty acid oxidation exceeds oxygen
A The rate of glycolysis exceeds oxygen availability B
availability
The rate of fatty acid oxidation exceeds the rate of The rate of carbohydrate breakdown exceeds the
C D
glycerol synthesis rate of protein synthesis
The rate of fatty acid oxidation exceeds the rate of
E
carbohydrate breakdown
Explanation
FATTY ACID OXIDATION *****
 If the rate of fatty acid oxidation exceeds the rate of carbohydrate breakdown, more acetyl CoA is
generated than can be converted to oxaloacetate - acetyl CoA is then converted to ketone bodies:
acetoacetate and hydroxybutyrate *
 Ketone bodies are produced mainly by the liver and used as fuel particularly by the heart, muscle and
renal cortex. During starvation, the brain may also utilise ketone bodies. The brain, however, metabolises
mainly glucose *
 After a three-day fast, 30% of the energy used by the brain is from ketone bodies. And after 40 days, this
goes up to 70%
 Both acetoacetate and beta-hydroxybutyrate are acidic, and if levels of ketone bodies are too
high,ketoacidosis occurs. This happens in untreated Type I diabetes and in alcoholics after binge
drinking and subsequent starvation*
 Ketone bodies are water soluble and may be excreted in the breath (acetone) or in urine causing
ketonuria *
 The fetal brain is an obligate glucose user and cannot utilise ketone bodies *
Question 49 Ketone bodies include
Acetic acid, acetoacetate and beta-

A Acetone, acetic acid and acetoacetate B
hydroxybutyrate
Acetyl CoA, acetoacetate and beta-
C D Glycerol, acetoacetate and acetone
hydroxybutyrate
E Acetone, acetoacetate and beta-hydroxybutyrate
Explanation
Question 50 In the post-absorptive phase of starvation

A Glycogen synthase is activated B Phosphorylase is activated
There is de-phosphorylation of key enzymes
C D Hormone-sensitive lipase is inactivated
involved in carbohydrate metabolism
E Glucose is absorbed from the blood into the liver

Explanation
STARVATION
POST-ABSORPTIVE PHASE
· Insulin concentrations fall while glucagon concentrations rise *
· Phosphorylation of enzymes occurs: Glycogen synthase -inactivated, glycogen phosphorylase -
activated, hormone sensitive lipase - activated *
· Triglyceride breakdown is stimulated in adipose tissue and glycogenolysis is stimulated with the
release of glucose and fatty acids into blood. *
Question 51 During the ketotic phase of starvation
A Ketone bodies inhibit insulin secretion B Insulin secretion is increased

C Acetoacetate is converted to acetyl CoA D The liver uses ketone bodies as fuel
E Protein hydrolysis is accelerated
Explanation
KETOTIC PHASE
· Acetyl CoA in the liver is converted to ketone bodies which are used as fuel mainly by the heart
and renal cortex
· Ketone bodies stimulate insulin secretion which prevents excessive protein hydrolysis
Question 52 During the digestion of protein

Pepsinogen is produced by the oxyntic cells of the Pepsinogen is converted to pepsin by
A B
stomach phosphorylation
Pepsinogen is converted to pepsin by the rise in
C D Pepsin is converted to pepsinogen
pH within the stomach
E Pepsin is an endopeptidase
Explanation
PROTEIN DIGESTION
MOUTH -mechanical disintegration only
STOMACH
· HCL secreted by Oxyntic cells denatures proteins
· Pepsinogen is secreted by Chief cells - converted into active pepsin when pH falls < 5
(autocatalysis) and by proteolysis by pepsin. Endopeptidase and cleaves peptide bonds on the NH2 side
of aromatic amino acids. Optimal pH = 2-3

Question 53 During the digestion of protein, enterokinase
A Is produced by the stomach B Converts pepsinogen to pepsin

C Converts trypsinogen to trypsin D Is produced by chief cells in the duodenum
E Is produced by oxyntic cells in the duodenum
Explanation
SMALL INTESTINE
· Enterokinase - secreted by duodenal mucosa: proteolytic conversion of trypsinogen to trypsin
· Bicarbonate secreted by the pancreas and biliary tree provides the optimal pH for enzyme action
· Trypsin also activates trypsinogen in addition to other zymogens including chymotrypsinogen, pro-
elastase and pro-carboxypeptidase
· Trypsin, chymotrypsin and elastase are endopeptidases - digest proteins from within the
polypeptide chain
· Carboxypeptidases release amino acids from the carboxy terminal of the polypeptide chain
· Endopeptidases, aminopeptidases and dipeptidases are present in the brush-border of intestinal
epithelial cells and hydrolyse oligopeptides
· Amino acids, dipeptides and tripeptides are absorbed. Further breakdown of di- and tri-peptides
occurs within intestinal epithelial cells
Question 54 Which enzyme does not play a role in the digestion of protein?
A Pepsin B Trypsin
C Elastase D Amylase
E Enterokinase
Explanation

AMINO ACIDS & PROTEINS

A DNA has a left-handed double helix structure B The DNA helix has 12 bases per turn
Heating to 90 degrees C causes irreversible
C The DNA helix completes a turn every 20 nm D
denaturation of DNA
Complementary nucleotides are held together
E
by hydrogen bonds
Explanation
RNA is single stranded while DNA has a double helix structure with purine pairing with pyrimidine bases
(A with T, G with C).* Complementary nucleotides are held together by non-covalent forces -mainly
hydrogen bonds and the two chains can be separated by heating to 90C. This process is reversible and
the two strands re-anneal on cooling *
· The double helix is right-handed with 10 bases per turn and a complete turn every 3.4nm
Histones are integral to the structure of the chromosome. Which one is the linker
Question 2
histone(s)
A H2A B H2B and H3

E H1 and H5
Explanation
The DNA in chromosomes is associated with several proteins, of which histones are the most abundant
· HISTONES are highly basic, positively charged arginine / lysine rich proteins which interact with the
negatively charged phosphate groups on DNA
· Histones H2A, H2B, H3 and H4 are known as the core histones, while histones H1 and H5 are
known as the linker histones
· DNA is wound around a histone octamer made up of two molecules of H2A, H2B,H3 & H4 to form
beads called nucleosomes
· Nucleosomes are joined by threads of double stranded (linker) DNA which is bound to histone H1/5
giving a -beads on a string- appearance


Explanation
MESSENGER RNA
· Single stranded and monocistronic (one mRNA molecule only codes for one protein). Synthesized
from DNA in the process of transcription by RNA polymerase. Mature mRNA does not contain introns and
exons - introns are removed during splicing before transport into the cytoplasm *
· Sequence is written in 5- to 3- direction. Has a 5- methylated cap followed by a leader sequence
then the start codon (AUG) followed by the translated region and the 3- poly-A tail *
Question 4 Messenger RNA

A Cannot be detected by Northern blotting B Can be detected by Western blotting
C Can be detected by Southern blotting and PCR D Cannot be detected by PCR
E Can be detected by Northern blotting and PCR
Explanation
Question 5 During transcription

Both the sense and the anti-sense DNA strands are
A A primer is required for mRNA synthesis B
transcribed
C Only the sense DNA strand is transcribed D The mRNA is synthesized in the 5- to 3- direction
E Any incorrect bases are removed by nucleases
Explanation
TRANSCRIPTION
· Process by which the genetic information in DNA is converted to RNA. Occurs in the nucleus *
· Catalysed by RNA polymerases *
· RNA polymerase I - synthesizes rRNA

· RNA polymerase II - synthesizes mRNA
· RNA polymerase III - synthesizes rRNA and tRNA
· Only the anti-sense DNA strand is transcribed. The mRNA molecule is synthesized in the 5- to 3-
direction
· RNA polymerase does not have a nuclease activity and cannot remove any incorrect bases. A
primer is not required for RNA synthesis *
The polymerase chain reaction is used to amplify DNA sequences. The DNA
Question 6
product is then identified using

A Western blotting B Northern blotting
C Restriction endonucleases D Light microscopy
E Fluorescent in-situ hybridization
Explanation
POLYMERASE CHAIN REACTION - PCR
• Enables the rapid amplification of DNA sequences in small biological samples *
• Used for pre-natal diagnosis and forensic medicine *
• Based on the use of DNA polymerases which function at high temperatures *
• Require the presence of DNA primers which flank the DNA sequence to be amplified and
deoxyribonucleotides
• Begins with the denaturation of DNA by heating to 90C *
• Primers anneal to the sequences to be amplified at 50C
• Extension of the primer sequence occurs at 70C
• The sequence is repeated usually over 30-35 cycles
• The DNA is separated by electrophoresis and the amplified sequences are visualised *
• Based on the primers used, the size of the PCR product can be predicted and this is used in
identification
• Further identification of PCR products requires sequencing to confirm their identity or use of
restriction endonucleases which should cut the sequence at a predicted point, with products of
predictable sizes *
Question 7 Restriction endonucleases

A Are enzymes B Are phospholipids
C Are histones D Produce Okazaki fragments
E Are used in the polymerase chain reaction
Explanation
RESTRICTION ENDONUCLEASES
• Enzymes which recognise specific DNA sequences and cut DNA at specific sites *
• Recognise palindromic sequences - sequences that are identical when read from left to right and
from right to left - AATTAA

• Cut DNA leaving 'blunt' ends - no bases sticking out, or 'sticky' ends with bases sticking out,
allowing complementary pairing with another chain
• May be used for the identification of PCR products as they cut at predictable sites, and should
produce fragments of predictable sizes if the identity of the PCR product is correct *
Question 8 Aliphatic amino acids include
A Arginine and lysine B Aspartate and glutamate

C Alanine and valine D Taurine and methionine
E Glutamine and cysteine
Explanation
synthesis.Cystathionase, is the enzyme that is necessary to convert cystathionine into cysteine, and is
present in humans post-natally *
Transamination of amino acids requires the presence of a prosthetic group

Question 9
derived from

A Vitamin K B Folic acid
C Vitamin B12 D Vitamin B6
E Vitamin C
Explanation
AMINO ACID METABOLISM
· Excess amino acids are neither stored nor excreted but are converted into glucose, fatty acids or
ketone bodies or oxidised for ATP production
· The initial process of amino acid catabolism is transamination -the alpha amino group is transferred
to alpha-ketoglutarate, converting it to glutamate with the formation of the corresponding alpha-keto-acid
· Transamination is catalysed by aminotransferases which are dependent on a pyridoxal phosphate
prosthetic group (derived from vitamin B6) *
· Alpha-keto-acids are converted into glucose (glucogenic amino acids) or ketone bodies (ketogenic
amino acids) *
· Leucine and lysine are the only strictly ketogenic amino acids *
· Isoleucine, tryptophan, phenylalanine and tyrosine are ketogenic and glucogenic *

· The other amino acids are glucogenic *
· During starvation, muscle protein is broken down into amino acids which are de-aminated and
metabolised into pyruvate. Pyruvate can be converted into alanine, transported to the liver and used for
gluconeogenesis *
· Amino acids are filtered in the glomerullus and actively absorbed in the proximal convoluted tubule *
Question 10 Strictly glucogenic amino acids include

A Alanine and valine B Leucine and lysine
C Tyrosine and alanine D Phenylalanine and lysine
E Arginine and lysine
Explanation
Question 11 Collagen fibrils are made up of alpha chains held together by

Cross-linking between proline and hydroxy-proline
A B Cross-linking between cysteine residues
residues
Cross-linking between lysine and hydroxy-lysine
C Cross-linking between methionine residues D
residues
E Cross-linking between cysteine and methionine residues
Explanation
Glycosylation of alpha chains occurs and three chains are intertwined to form a right handed triple helix *-
tropocollagen which is released into the extracellular matrix
· The propeptide in most forms of collagen is excised in the extracellular matrix and tropocollagen
molecules spontaneously aggregate to form polymeric fibrils held together through cross-linking between
lysine and hydroxylysine residues. These have a banded appearance on electron microscopy *
Proteins are synthesised from amino acids using the genetic code. Each
Question 12
codon is made up of

A 2 bases B 3 bases
E 3 base pairs

Explanation
THE GENETIC CODE *****

Triplet codon derived from 4 bases giving a total of 64 possible codons
There are 20 amino acids, each coded by a different specific codon
However, one amino acid can have more than one codon - the genetic code is DEGENERATE *
Question 13 Uric acid

A Is produced from the breakdown of proteins in the liver B Is produced from the breakdown of purines in the spleen
Is produced from the breakdown of pyrimidines in the
C D Is produced from the breakdown of purines in the liver
liver
Is produced from the breakdown of nucleotides in
E
reticulo-endothelial cells
Explanation
URIC ACID *****
· Plasma concentration higher in males (202 - 406 microM) than in females (148 - 357 microM) *
· Weak acid with a pK of 5.8. At pHs below the pK, it exists predominately in a nonionized form
· The renal tubule can reabsorb or secrete. Typically, net reabsorption occurs in infants and children
while net secretion occurs in adults *
· The kidneys excrete two-thirds of the uric acid produced daily; the remaining one-third is excreted in
the stool
· In early pregnancy uric acid levels fall by about one-third but rise to non-pregnant levels by term *
Question 14 During the urea cycle

A 1 molecule of ATP is produced per molecule of urea B 2 molecules of ATP are consumed per molecule of urea
C 3 molecules of ATP are produced per molecule of urea D 2 molecules of ATP are produced per molecule of urea
E 3 molecules of ATP are consumed per molecule of urea
Explanation
Fumarate formed in the urea cycle can enter the citric acid cycle
· 3 molecules of ATP are consumed per molecule of urea formed in the urea cycle

Question 15 With respect to monosaccharides

A Glucose is a hexose and a ketose B Glucose is a hexose and an aldose
C Glucose is a pentose and an aldose D Glucose is a pentose and a ketose
E Glucose is a hexose and can be an aldose or a ketose
Explanation
MONOSACCHARIDES *****
· Have a general formula (CH2O)n where n is 3 or more
· Have an aldehyde (aldose) or ketone (ketose) group *
· The free aldehyde or ketone can reduce Cu2+ to Cu+ - this forms the basis of Fehling’s and
Benedict’s tests. All monosaccharides are reducing sugars
· Include glucose, fructose, galactose
· Carbon atoms are numbered beginning with the C carrying the aldehyde or ketone group
· Glucose is an aldose while fructose is a ketose *
· Glucose has 6 carbon atoms and is therefore a hexose *
· D and L forms refer to the configuration of the asymmetry of the C atom furthest away from the
aldehyde or ketone group *

A Glucagon inhibits glycogenolysis B Glucagon stimulates glycogen synthesis
C Calcium ions inhibit glycogenolysis D Calcium ions stimulate glycogen synthesis
Glucagon stimulates the phosphorylation of
E
phosphorylase b
Explanation

 Regulated by the phosphorylation and dephosphorylation of phosphorylase (glycogenolysis) and
glycogen synthase (glycogen synthesis)
 Phosphorylase exists as a phosphorylated active 'a' form and a dephosphorylated inactive 'b' form
 Glycogen synthase exists as a phosphorylated INACTIVE 'b' form and a dephosphorylated active 'a' form
 Phosphorylation / dephosphorylation is regulated by the activity of phosphorylase kinase and protein
phosphatase I
 GLUCAGON / ADRENALINE - stimulate the phosphorylation of inactive phosphorylase ′ b′, converting it
into active phosphorylase ′a′ and glycogenolysis is stimulated *
 Phosphorylation of glycogen synthase converts the active 'a' form to the inactive 'b' form and glycogen
synthesis is inhibited
 Phosphorylated and active phosphorylase 'a' is de-phophorylated and inactivated - glycogenolysis is
inhibited *
 Phosphorylated and inactive glycogen synthase 'b' is dephosphorylated and activated - glycogen
synthesis is activated *

 Calcium ions released during muscle contraction stimulate glycogenolysis. Skeletal muscle glycogen
cannot be converted into glucose. *

Explanation
GLYCOLYSIS *****
 Occurs in the cytoplasm and does not require oxygen. Principal energy generating mechanism in the
absence of oxygen of in cells such as RBC which do not have mitochondria *
 Initial reactions involve two phosphorylation steps: initially by hexokinase to form glucose-6-phosphate
(converted to fructose-6-phosphate by isomerase) and then to fructose 1,6 bisphosphate by
phosphofructokinase with the hydrolysis of ATP to ADP

Question 18 The enzyme phosphofructokinase plays a key role in

A Gluconeogenesis B Glycolysis
C Glycogen synthesis D Glycogenolysis
E The Cori cycle
Explanation


Explanation
FATTY ACID SYNTHESIS *****
 Takes place in the cytosol
 Mediated by a single polypeptide enzyme - fatty acid synthase with several enzymatic domains
 The committed step in the pathway is the conversion of acetyl CoA to malonyl CoA by acetyl CoA
carboxylase
 Occurs by the repetitive addition of two carbon units from malonyl CoA which has a three carbon unit,
with the release of CO2
ATP is consumed during fatty acid synthesis
Question 20 The breakdown of triglycerides occurs in

A The cytoplasm B The lysosomes
Explanation

A Acetone, acetic acid and acetoacetate B Acetic acid, acetoacetate and beta-hydroxybutyrate
C Acetyl CoA, acetoacetate and beta-hydroxybutyrate D Glycerol, acetoacetate and acetone
Explanation
 If the rate of fatty acid oxidation exceeds the rate of carbohydrate breakdown, more acetyl CoA is
generated than can be converted to oxaloacetate - acetyl CoA is then converted to ketone bodies:
acetoacetate and hydroxybutyrate *
 Ketone bodies are produced mainly by the liver and used as fuel particularly by the heart, muscle and
renal cortex. During starvation, the brain may also utilise ketone bodies. The brain, however, metabolises
mainly glucose *
 After a three-day fast, 30% of the energy used by the brain is from ketone bodies. And after 40 days, this
goes up to 70%
high,ketoacidosis occurs. This happens in untreated Type I diabetes and in alcoholics after binge
drinking and subsequent starvation*
 Ketone bodies are water soluble and may be excreted in the breath (acetone) or in urine causing
ketonuria *


Explanation
KETOTIC PHASE
· Acetyl CoA in the liver is converted to ketone bodies which are used as fuel mainly by the heart
and renal cortex

Pepsinogen is produced by the oxyntic cells of the
A B Pepsinogen is converted to pepsin by phosphorylation
stomach
Pepsinogen is converted to pepsin by the rise in pH
within the stomach
Explanation
PROTEIN DIGESTION
STOMACH
(autocatalysis) and by proteolysis by pepsin. Endopeptidase and cleaves peptide bonds on the NH2 side
of aromatic amino acids. Optimal pH = 2-3

Explanation
SMALL INTESTINE
· Enterokinase - secreted by duodenal mucosa: proteolytic conversion of trypsinogen to trypsin
· Bicarbonate secreted by the pancreas and biliary tree provides the optimal pH for enzyme action

· Trypsin also activates trypsinogen in addition to other zymogens including chymotrypsinogen, pro-
elastase and pro-carboxypeptidase
polypeptide chain
· Carboxypeptidases release amino acids from the carboxy terminal of the polypeptide chain
· Endopeptidases, aminopeptidases and dipeptidases are present in the brush-border of intestinal
epithelial cells and hydrolyse oligopeptides
· Amino acids, dipeptides and tripeptides are absorbed. Further breakdown of di- and tri-peptides
occurs within intestinal epithelial cells
A Pepsin B Trypsin
E Enterokinase
Explanation
Question 26 Enzymatic digestion of carbohydrates

A Occurs in the mouth, stomach and small intestines B Occurs in the stomach and small intestines only
C Does not occur in the stomach D Is undertaken by amylase and pepsin
E Is undertaken by pepsinogen and trypsinogen
Explanation
CARBOHYDRATE DIGESTION *****
MOUTH
· Salivary amylase, hydrolyses alpha 1,4 glycosydic bonds
· Salivary amylase is inactivated by the acidic environment in the stomach. Enzymatic digestion of
carbohydrates does not occur in the stomach
· Pancreatic amylase is secreted by the pancreas and continues the hydrolysis of glycosidic bonds.
Bicarbonate provides optimal pH for enzyme action
· Ologosaccharides and disaccharides are further digested by enzymes within the brush border of
intestinal epithelial cells: Sucrase: sucrose to glucose + fructose; Lactase: Lactose to glucose +
galactose; Maltase: maltose to glucose
· Lactase deficiency results in impaired lactose digestion. Lactose is fermented by bacteria in the
colon producing gas and osmotically active products which cause flatulence and diarrhoea


Question 27 Essential amino acids include

A Methionine, serine and taurine B Leucine, isoleucine and lysine
C Lysine, arginine and taurine D Methionine, phenylalanine and alanine
E Histidine, valine and tyrosine
Explanation
ESSENTIAL AMINO ACIDS
These are amino acids which cannot be synthesised by the body and must be absorbed from
the diet
Include: Histidine, Leucine, Isoleucine, Lysine, Methionine, Phenylalanine, Threonine,
Tryptophan, Valine *
Question 28 Which one is an aromatic amino acid?

A Alanine B Arginine
C Taurine D Serine
E Tyrosine
Explanation
synthesis.Cystathionase, is the enzyme that is necessary to convert cystathionine into
cysteine, and is present in humans post-natally *

Question 29 Which amino acids are converted to cysteine in the human adult liver?

A Serine and valine B Arginine and lysine
C Glutamine and lysine D Histidine and proline
E Methionine and serine
Explanation
Question 30 Cystathionase

A Is abundant in the human fetal liver B Is abundant in the human fetal brain
C Converts cysteine to methionine D Converts cystathionine to cysteine
E Is not present in the adult human liver
Explanation
Question 31 Which one is an essential amino acid in the fetus but not the adult?

A Arginine B Valine
C Cysteine D Methionine
E Phenylalanine
Explanation
Cysteine is not an essential amino acid in adults but is an essential amino acid for the human
fetus, and for prematurely born and full term infants for a short period after birth. *
· Cysteine concentration in maternal plasma is greater than or equal to that in fetal plasma
· Methionine is also a precursor for taurine synthesis
Question 32 The first step in amino acid catabolism is


Explanation
AMINO ACID METABOLISM
· Excess amino acids are neither stored nor excreted but are converted into glucose, fatty
acids or ketone bodies or oxidised for ATP production
· The initial process of amino acid catabolism is transamination -the alpha amino group is
transferred to alpha-ketoglutarate, converting it to glutamate with the formation of the
corresponding alpha-keto-acid
· Transamination is catalysed by aminotransferases which are dependent on a pyridoxal
phosphate prosthetic group (derived from vitamin B6) *
· Alpha-keto-acids are converted into glucose (glucogenic amino acids) or ketone bodies
(ketogenic amino acids) *
· Leucine and lysine are the only strictly ketogenic amino acids *
· Isoleucine, tryptophan, phenylalanine and tyrosine are ketogenic and glucogenic *
· The other amino acids are glucogenic *
· During starvation, muscle protein is broken down into amino acids which are de-aminated
and metabolised into pyruvate. Pyruvate can be converted into alanine, transported to the liver
and used for gluconeogenesis *
· Amino acids are filtered in the glomerullus and actively absorbed in the proximal
convoluted tubule *
Question 33 Strictly ketogenic amino acids include

A Leucine and arginine B Alanine and arginine
C Serine and valine D Methionine and cysteine
E Leucine and lysine
Explanation
Amino acids are small molecules which are filtered in the glomerulus. The amino
Question 34
acids are than absorbed
By facilitated diffusion in the distal convoluted By active transport in the proximal convoluted
A B
tubule tubule
C By diffusion in the proximal convoluted tubule D By active transport in the loop of Henle
E By facilitated diffusion in the loop of Henle
Explanation

Question 35 With respect to the structure of proteins

Haemoglobin does not have a quaternary Secondary structure is the linear sequence of
A B
structure amino acids including disulphide bonds
Secondary structure includes folding into pleated
C D Tertiary structure is dependent on covalent bonds
sheets
Tertiary structure is only present in proteins with
E
more than one sub-unit
Explanation
PROTEIN STRUCTURE
· Primary structure - linear sequence of amino acids, including disulphide bonds
· Secondary structure - protein folding into alpha helix and pleated sheets
· Tertiary structure - regional folding between alpha helix and pleated sheets - dependent
on non-covalent forces
· Quaternary structure - only present in proteins with more than one sub-unit - such as
haemoglobin
Question 36 With respect to the structure of collagen

Each collagen molecule has an alpha and a beta The collagen peptide has a right handed helical
A B
chain structure
The collagen peptide is rich in cysteine and The collagen peptide is rich in proline and
C D
methionine hydroxyproline
E The collagen peptide does not contain lysine
Explanation
Each collagen peptide is referred to as an alpha chain and is a left handed helical polypeptide
with the basic structure (Gly-A-B) n where one third of A residues are proline and one third of B
residues are hydroxyproline. Collagen is also rich in lysine and hydroxylysine *
The alpha chain of collagen has the basic structure Gly-A-B. One in three A
Question 37
residues are

A Cysteine B Methionine
C Valine D Proline
E Hydroxy-proline

Explanation
Question 38 Collagen fibrils contain

A Three alpha chains B Five alpha chains
C One alpha and two beta chains D Two alpha and one beta chain
E Two alpha and two beta chains
Explanation
Glycosylation of alpha chains occurs and three chains are intertwined to form a right handed
triple helix *- tropocollagen which is released into the extracellular matrix
· The propeptide in most forms of collagen is excised in the extracellular matrix and
tropocollagen molecules spontaneously aggregate to form polymeric fibrils held together
through cross-linking between lysine and hydroxylysine residues. These have a banded
appearance on electron microscopy *

Type II collagen has a left-handed triple helix
A Type 1 collagen has a double helix structure B
structure
All types of collagen have a right handed triple
C D Type IV collagen does not have a helical structure
helix structure
Type II and IV collagen have a right handed
E
double helix structure
Explanation

Collagen fibrils are visible under the light Collagen fibrils have a banded appearance on
A B
microscope electron microscopy
Collagen fibres are not visible under the light
C D Collagen fibres aggregate to form collagen fibrils
microscope
E All collagen fibrils have a double helix structure

Explanation
Question 41 Type I collagen

A Contains three different alpha chains B Contains two beta chains
Contains two identical and one different alpha
C Is found in bone, cartilage and skin D
chain
E Is not found in the skin
Explanation
Collagen type I: two identical and one different alpha chain. Makes up 90% of total collagen and
is found in skin, bone, tendon *
· Collagen type II: three identical alpha chains - cartilage and inter-vertebral disc *
· Collagen type III: three identical alpha chains - interstitial collagen in skin and organs *
· Collagen type IV: two identical and one different alpha chain - basement membrane *
Question 42 Type III collagen

A Has two alpha chains B Has two identical and one different alpha chain
Has three identical alpha chains and is found in Has three different alpha chains and is found in
C D
the inter-vertebral disc skin
Has three identical alpha chains and is found in
E
skin
Explanation
Question 43 Which one is the predominant type of collagen found in basement membranes?

A Type I B Type II
C Type III D Type IV
E Type V

Explanation
Collagen type I: two identical and one different alpha chain. Makes up 90% of total collagen
and is found in skin, bone, tendon *
Question 44 Which one is not a recognised stage during protein synthesis from mRNA?

A Initiation B Transcription
C Elongation D Translocation
E Termination
Explanation
PROTEIN SYNTHESIS
Occurs in the RIBOSOMES within the cytoplasm during TRANSLATION *
Four stages: initiation, elongation, translocation, termination.
Question 45 With respect to protein synthesis and the genetic code

A There are 96 possible codons B Each codon has 4 bases
Some codons recognise more than one amino Some amino acids are recognised by more than
C D
acid one codon
E Some codons have 5 bases
Explanation

Question 46 During translation

The mRNA molecule is translated from the 3-end
A B ATP is not required
to the 5-end
Amino acids have to be bound to tRNA before Amino acids must be bound to mRNA before they
C D
they can be added to the protein chain can be added to the protein chain
Amino acids have to be transferred into the
E endoplasmic reticulum before they can be added
to the protein chain
Explanation
The mRNA molecule is translated from the 5- end to the 3- end
• For an amino acid to be added to the protein chain, it must be bound to a tRNA molecule
in a reaction catalysed by aminoacyl tRNA synthetase. There are 20 enzymes, each specific for
a particular amino acid. During this reaction, ATP is hydrolysed to AMP + 2Pi *
• The binding of tRNA molecules to the mRNA molecule is less stringent than the pairing of
complementary DNA strands. Pairing may still occur when the third position on the mRNA
codon read from the 5- to 3- end and the first position on the anticodon on the aminoacyl-tRNA
is not an exact match: the WOBBLE hypothesis
Question 47 During protein synthesis

New amino acids are added at the P site of the
A Elongation is catalysed by peptidyl transferase B
ribosome
Once the peptide bond is formed, there is a
C checking mechanism to remove wrong amino D The termination codon is AUG
acids
The polypeptide chain is synthesised from C- to
E
N- terminal
Explanation
ELONGATION - two processes - peptide bond formation and translocation
• New aminoacyl-tRNAs are added to the A site and a peptide bond is formed between the
carbonyl atom of the P site aminoacyl tRNA and the alpha amino group of the A site amino acid
- catalysed by PEPTIDYL TRANSFERASE
• There are mechanisms to check that the correct aminoacyl-tRNA is added to the A site.
Once the peptide bond is formed, the wrong amino acid cannot be removed
• Translocation is the process of movement down the mRNAmolecule so that the A site is
emptied for the next aminoacyl-tRNA - mediated by TRANSLOCASE and GTP hydrolysis
• TERMINATION - a termination code (UGA, UAA, UAG) is encountered. Peptidyl
transferase switches to a hydrolase function and hydrolyses the carbonyl end of the peptide
chain. Release factors catalyse the release of the peptide chain from the ribosomal complex
which dissociates.
• The polypeptide chain is synthesized from the N- to the C- terminal *

Post-translational modification of proteins include excision of signal sequences.
Question 48
Signal sequences

A Are only present in hormones B Play an important role in cell signaling
Are only present in proteins destined for export
C Target the proteins to specific sites within the cell D
into the extra-cellular space
E Are removed in the ribosomes
Explanation
POST-TRANSLATIONAL MODIFICATIONS *****
• Excision of signal sequences - these sequences target proteins to specific sites,
mitochondria for instance and are removed once the target is reached. Nuclear proteins have
arginine and lysine -rich sequences
• Disulphide bond formation
• Proteolysis - for instance the conversion of pro-hormones to hormones
• Glycosylation - three types: N-linked; O-linked and addition of the glycosyl
phosphatidylinositol anchor to membrane proteins
• O-linked glycosylation occurs by the sequential addition of monosaccharide units to the
OH group of serine or threonine sidechains
• N-linked glycosylation is the addition of oligosaccharide molecules to the NH2 groups of
asparagine sidechains
• Proteins may be modified during translation - for instance proline is hydroxylated during
collagen synthesis
Question 49 In the human adult, uric acid levels

A Are higher in women than in men B Fall in early pregnancy
C Increase slightly in early pregnancy D Double by 12 weeks gestation
Are 50% lower in the term normal pregnancy
E
compared to outside pregnancy
Explanation
URIC ACID *****
· Plasma concentration higher in males (202 - 406 microM) than in females (148 - 357
microM) *
· Weak acid with a pK of 5.8. At pHs below the pK, it exists predominately in a nonionized
form

· The renal tubule can reabsorb or secrete. Typically, net reabsorption occurs in infants and
children while net secretion occurs in adults *
· The kidneys excrete two-thirds of the uric acid produced daily; the remaining one-third is
excreted in the stool
· In early pregnancy uric acid levels fall by about one-third but rise to non-pregnant levels
by term *
Question 50 Which one is associated with raised plasma uric acid concentrations?

A Starvation B Use of allopurinol
C Use of probenecid D High vitamin C intake
E Poor dietary intake of purines
Explanation
Causes of raised Plasma uric acid concentration *****
· Renal diseases with renal failureand prerenal renal failure (e.g. dehydration)
· Gout.
· Drugs - diuretics, pyrazinamide, ethambutol, nicotinic acid, and aspirin in low doses. *
· Excessive cell death - neoplasia, even before as well as following chemotherapy and
radiotherapy, especially lymphoma and leukemia; hemolytic anemia, resolving pneumonia and
other inflammation; polycythemia, myeloma, pernicious anemia, infectious mononucleosis,
congestive heart failure, large myocardial infarct. *
· Endocrine conditions: hypothyroidism, hypoparathyroidism, hyperparathyroidism,
pseudohypoparathyroidism; diabetes insipidus of nephrogenic type, Addison disease.
· Lead poisoning
· Hyperlipidaemia
· Acidosis: lactic acidosis, diabetic ketoacidosis, alcoholic ketosis.
· Pre-eclampsia *
· Dieting, weight loss, fasting or starvation. *
· Decreased urate clearance: cyclosporine-induced hyperuricemia.
Low uric acid concentration *****

· Drugs - allopurinol, corticosteroids and probenecid cause low uric. Massive doses of
vitamin C are uricosuric
· Poor dietary intake of purines and protein; tea, coffee.
· Renal tubular defects, Fanconi syndrome, late in Wilson disease

Question 51 Which molecule has formula CO(NH2)2?

A Uric acid B Urea
C Urate D Acetyl CoA
E Acetate
Explanation
UREA *****
· Excess nitrogen is converted to ammonia and excreted as urea which is formed in the
urea cycle
· Molecule contains two amine groups {CO(NH2)2}*
· The urea cycle occurs in the liver. Blood urea is then taken up and excreted by the
kidneys
Question 52 The reactions of the urea cycle occur

A In the mitochondria B In the cytoplasm
C In the mitochondria and the cytoplasm D In the rough endoplasmic reticulum
E In the lysosomes
Explanation
Ammonia is conbined with CO2 to form carbamoyl phosphate
· Carbamoyl phosphate conbines with orinthine to form citrulline. Citrulline + aspartate to
form arginosuccinate
· Arginosuccinate splits to release arginine and fumarate
· Arginine then splits to form urea and regenerate ornithine
· First 2 reactions occur in the mitochondria, rest occur in cytosol

C D
Explanation

· About 50% of the filtered urea is reabsorbed passively in the proximal tubule by a
paracellular route
· Urea is secreted into the tubule fluid in the descending limb of the loop of Henle by carrier
mediated transport *
· Final urea excretion is dependent on the additional amount reabsorbed by carrier-
mediated transport in the medullary collecting ducts. This reabsorption increases at low urine
flows and decreases at high urine flows and is controlled by ADH. *

E The renal pelvis
Explanation
Question 55 Plasma urea concentration

A Decreases with age B Increases with age
C Is higher in women than in men D Is increased in people on a low protein diet
E Is undetectable during fetal life
Explanation
Urea concentration increases with age and is higher in males than in females
· The urinary excretion of urea is proportional to protein intake and is increased on a high
protein diet. Urea excretion is decreased during growth and pregnancy or due to action of
insulin, growth hormone and testosterone *
· The enzyme system necessary for urea synthesis in human fetuses is functional when
mesonephric glomeruli are present and urea is produced by the fetus *
Question 56 Urea excretion is increased

A During pregnancy B By insulin
C By consuming a high protein diet D By testosterone
E By growth hormone
Explanation

CARBOHYDRATE & LIPID METABOLISM

A Purine bases include guanine and thymine B Purine bases include thymine and cytosine
C Pyrimidine bases include ribose and deoxyribose D Pyrimidine bases include thymine and cytosine
E Uracil is both a purine and a pyrimidine base
Explanation
NUCLEOTIDES
· Base - purine (guanine -G and adenine -A) or pyrimidine (thymine -T, cytosine -C and
uracil -U) *
· Pentose (5-carbon) sugar - ribose (RNA) or deoxyribose (DNA) Phosphate *
· Uracil is found only in RNA and replaces thymine *
· Nucleotides are linked by 3-5-phosphodiester bonds to form nucleic acids. The 3-end of
the chain has a free OH group while the 5- end has a phosphate group. During synthesis,
nucleotides are added to the 3- end
Histones are integral to the structure of the chromosome. Which one is the
Question 2
linker histone(s)

A H2A B H2B and H3
E H1 and H5
Explanation
The DNA in chromosomes is associated with several proteins, of which histones are the most
abundant
histone H1/5 giving a -beads on a string- appearance


A 10 : 1 B 5:1
C 2:1 D 1:1
E 0.1 : 1
Explanation

Explanation
MESSENGER RNA
cytoplasm *

Explanation

Question 6 Which one is not an essential amino acid?

A Arginine B Leucine
C Lysine D Tryptophan
E Valine
Explanation
ESSENTIAL AMINO ACIDS
These are amino acids which cannot be synthesised by the body and must be absorbed from
the diet
Include: Histidine, Leucine, Isoleucine, Lysine, Methionine, Phenylalanine, Threonine,
Tryptophan, Valine

Explanation

Question 8
residues are

C Valine D Proline
E Hydroxy-proline
Explanation

residues
residues
Cross-linking between cysteine and methionine
E
residues
Explanation

E Termination
Explanation
PROTEIN SYNTHESIS

Question 11 Aminoacyl tRNA synthetase plays a key role in protein synthesis.

A There are 5 different enzymes B The reaction catalysed results in ATP production
The reaction catalysed results in the formation of
C There are 20 different enzymes D
disulphide bonds
There are 3 different enzymes – alpha, beta and
E
gamma
Explanation
A Uric acid B Urea

E Acetate
Explanation
UREA *****
urea cycle
kidneys
C D

Explanation
paracellular route

E The renal pelvis
Explanation
paracellular route
Question 15 Plasma urea concentration

A Decreases with age B Increases with age
C Is higher in women than in men D Is increased in people on a low protein diet
E Is undetectable during fetal life
Explanation
Urea concentration increases with age and is higher in males than in females
· The urinary excretion of urea is proportional to protein intake and is increased on a high
protein diet. Urea excretion is decreased during growth and pregnancy or due to action of
insulin, growth hormone and testosterone *
· The enzyme system necessary for urea synthesis in human fetuses is functional when
mesonephric glomeruli are present and urea is produced by the fetus *

Question 16 With respect to monosaccharides

A Glucose is a hexose and a ketose B Glucose is a hexose and an aldose
C Glucose is a pentose and an aldose D Glucose is a pentose and a ketose
Glucose is a hexose and can be an aldose or a
E
ketose
Explanation
· The free aldehyde or ketone can reduce Cu2+ to Cu+ - this forms the basis of Fehling’s
and Benedict’s tests. All monosaccharides are reducing sugars
· D and L forms refer to the configuration of the asymmetry of the C atom furthest away
from the aldehyde or ketone group *
Question 17 Nascent high density lipoprotein

A Is produced by adipose tissue B Is produced in the gut
C Is produced by the liver D Has a protein content of 10-20%
E Has triglycerides as the major lipid component
Explanation
Nascent HDL *****
· Produced by the liver. * More HDL is formed within the circulation. *
· Molecular weight 175-360Da, density 1.063 - 1.21g/ml
· 40-55% protein.*
· Major lipids are phospholipids and cholesterol ester *
· HDL extracts cholesterol from cell membranes, converting it into cholesterol esters which
are then transferred to VLDL. VLDL and HDL are taken up by the liver by receptor mediated
endocytosis and cholesterol is excreted in bile in the form of bile salts - the liver is the only
organ that can dispose of significant quantities of cholesterol. *

Question 18 With respect to the different lipoproteins

A HDL has the lowest protein content B VLDL has the highest density
All lipoproteins contain cholesterol and
C Chylomicrons are the smallest particle D
phospholipids
E Some lipoproteins do not contain proteins
Explanation
LIPOPROTEINS *****
· Globular particles consisting of a hydrophobic core and a hydrophilic surface. Contain

triglycerides, cholesterol, phospholipids, apoproteins
· Chylomicrons carry triglycerides from the intestines to the liver, skeletal muscle and
adipose tissue.
· Very-low-density lipoproteins (VLDL) carry (newly synthesised) triglycerides from the liver
to adipose tissue.
· Intermediate-density lipoproteins (IDL) are intermediate between VLDL and LDL. They
are not usually detectable in the blood when fasting.
· Low-density lipoproteins (LDL) carry 3,000 to 6,000 fat molecules (phospholipids,
cholesterol, triglycerides, etc.) around the body. LDL particles are sometimes referred to as
"bad" lipoprotein because concentrations, dose related, correlate with atherosclerosis
progression.
· High-density lipoproteins (HDL) collect fat molecules (phospholipids, cholesterol,
triglycerides, etc.) from the body's cells/tissues, and take it back to the liver. HDLs are
sometimes referred to as "good" lipoprotein because higher concentrations correlate with low
rates of atherosclerosis progression and/or regression

E
phosphorylase b
Explanation
 Regulated by the phosphorylation and dephosphorylation of phosphorylase (glycogenolysis)
and glycogen synthase (glycogen synthesis)

 Phosphorylase exists as a phosphorylated active 'a' form and a dephosphorylated inactive 'b'
form
 Glycogen synthase exists as a phosphorylated INACTIVE 'b' form and a dephosphorylated
active 'a' form
 Phosphorylation / dephosphorylation is regulated by the activity of phosphorylase kinase and
 GLUCAGON / ADRENALINE - stimulate the phosphorylation of inactive phosphorylase ′ b′,
converting it into active phosphorylase ′a′ and glycogenolysis is stimulated *
 Phosphorylation of glycogen synthase converts the active 'a' form to the inactive 'b' form
and glycogen synthesis is inhibited
 Phosphorylated and active phosphorylase 'a' is de-phophorylated and inactivated -
glycogenolysis is inhibited *
 Phosphorylated and inactive glycogen synthase 'b' is dephosphorylated and activated -
glycogen synthesis is activated *
 Calcium ions released during muscle contraction stimulate glycogenolysis. Skeletal muscle
glycogen cannot be converted into glucose. *

Explanation
GLUCONEOGENESIS *****
 Formation of glucose from non-carbohydrate precursors
 Occurs mainly in the liver but also in the renal cortex
Substrates include: *
1) Pyruvate 3) Oxaloacetate
2) Lactate 4) Some amino acids
5) Glycerol
Two molecules of pyruvate are converted to one molecule of glucose with the hydrolysis of 4
molecules of ATP and two molecules of GTP *
 Gluconeogenesis occurs during conditions of deficient dietary intake
Question 21 The fetal brain
A Can utilise ketone bodies as fuel B Only utilises glucose as fuel

C Can utilise glucose and ketone bodies as fuel D Only utilises ketone bodies as fuel
Can utilise ketone bodies as fuel if the woman
E
has type 1 diabetes

Explanation
 If the rate of fatty acid oxidation exceeds the rate of carbohydrate breakdown, more acetyl CoA
is generated than can be converted to oxaloacetate - acetyl CoA is then converted to ketone
bodies: acetoacetate and hydroxybutyrate *
 Ketone bodies are produced mainly by the liver and used as fuel particularly by the heart,
muscle and renal cortex. During starvation, the brain may also utilise ketone bodies. The brain,
however, metabolises mainly glucose *
 After a three-day fast, 30% of the energy used by the brain is from ketone bodies. And after 40
days, this goes up to 70%
high,ketoacidosis occurs. This happens in untreated Type I diabetes and in alcoholics after
binge drinking and subsequent starvation*
 Ketone bodies are water soluble and may be excreted in the breath (acetone) or in urine
causing ketonuria *

Explanation
KETOTIC PHASE
· Acetyl CoA in the liver is converted to ketone bodies which are used as fuel mainly by the
heart and renal cortex
Which one is not a product of intermediate molecules derived from the citric
Question 23
acid cycle?

A Fatty acids B Glucose
C Amino acids D Porphyrin
E Folic acid
Explanation
 The citric acid cycle also produces intermediates for other biosynthetic pathways. For instance:
*

1) Citrate for fatty acid synthesis
2) Alpha-ketoglutarate which is trans-aminated for amino acid synthesis
3) Alpha-ketoglutarate and oxaloacetate used for the synthesis of purines and pyrimidines
4) Oxaloacetate used for glucose synthesis - gluconeogenesis
5) Succinyl-coA used for the synthesis of the porphyrin ring of heme groups
Question 24 The velocity of an enzyme reaction

For a given concentration of enzyme, is
A Is lowest at time t = 0 B
proportional to the substrate concentration
C Is highest at time t = 0 D Is independent of the substrate concentration
E Is independent of the concentration of product
Explanation
ENZYME KINETICS
 VELOCITY: The rate of an enzyme-catalysed reaction. Highest at time t=0 (initial velocity, V0)
because the substrate concentration is maximum and there is no product formed (product may
have feed-back inhibition on enzyme activity)
 If the substrate concentration is progressively increased for a fixed enzyme concentration, there
comes a point where all the active sites on the enzyme are occupied and the initial velocity of
the reaction cannot be increased further. This is the maximum velocity Vmax
 If there is an excess of substrate, the initial velocity is proportional to the enzyme concentration
and vice-versa
 The initial velocity is given by the Michaelis-Menten equation:
V0 = (Vmax[S]) /([S] +Km): Km = Michaelis constant which is the substrate concentration at

which the initial velocity of the reaction is half the maximum velocity
Question 25 With respect to enzyme kinetics, the Michaelis constant is

The enzyme concentration at which the initial
A B The initial velocity at t = 0.5
velocity is half of Vmax
The substrate concentration at which the initial
C D velocity is proportional to the substrate
concentration
E
velocity is equal to Vmax
Explanation

Question 26 With respect to competitive and non-competitive enzyme inhibitors

Competitive inhibitors reduce the Km and the Non-competitive inhibitors reduce the Km but the
A B
Vmax of the enzyme Vmax is unchanged
Both competitive and non-competitive inhibitors Both competitive and non-competitive inhibitors
C D
increase the Km reduce the Vmax
Non-competitive inhibitors reduce the Vmax but
E
competitive inhibitors do not alter the Vmax
Explanation
COMPETITIVE INHIBITION
competes with the substrate for its binding site on the enzyme. Usually a substrate
analogue and may be converted to product. Action can be overcome by increasing
substrate concentration. There is an apparent increase in the Km of the enzyme (more
substrate required to achieve a particular initial rate) but no change in the Vmax. The
Lineweaver-Burk plot therefore shows no change in the intercept on the y-axis (1/Vmax)
BUT the slope (Km/Vmax) is increased
NON-COMPETITIVE INHIBITION
binds to the enzyme at a site other than the active site. The substrate may still bind to
the enzyme but is not converted to product. Enzyme is effectively removed from the
reaction. The Km is unchanged but the Vmax is reduced, hence the y-intercept and the
slope of the Lineweaver-Burk plot are both altered.

A B
Explanation
PROTEIN DIGESTION
STOMACH
(autocatalysis) and by proteolysis by pepsin. Endopeptidase and cleaves peptide bonds on the
NH2 side of aromatic amino acids. Optimal pH = 2-3

Question 28 The digestion of lipids

A Begins in the mouth B Does not occur in the stomach
C Is undertaken by amylase and lipase D Occurs in the mouth and stomach
E Begins in the stomach
Explanation
LIPID DIGESTION
· Begins in the stomach by the action of lingual lipase secreted by glands at the back of the
tongue and active in the acidic pH of the stomach. Hydrolyses triglycerides to fatty acids, mono -
/ di-acylglycerol and glycerol *
· Main enzymatic digestion of fats occurs in the small intestine
· Pancreas secretes pancreatic lipase, lipid esterase and phospholipase A2 with
bicarbonate providing the optimal pH for enzyme action. Pancreatic lipase is inhibited by bile
acids but activated by colipase -secreted by the pancreas as procolipase and activated by
trypsin. Lipid esterase and phospholipase A2 require bile acids for optimal function
N = 27
Question 29 Monosaccharides

A Include glucose and fructose but not galactose B Include glucose, fructose and maltose
C Are all reducing sugars D All have 6 carbon atoms
E Are always aldose sugars
Explanation
· The free aldehyde or ketone can reduce Cu2+ to Cu+ - this forms the basis of Fehling’s
and Benedict’s tests. All monosaccharides are reducing sugars
· D and L forms refer to the configuration of the asymmetry of the C atom furthest away
from the aldehyde or ketone group *

Question 30 Which hormone typically reduces plasma free fatty acid concentrations?

A Insulin B Glucagon
C Adrenalin D Noradrenalin
E Inhibin A
Explanation
TRIGLYCERIDES *****
· Three faty acid chains esterified to a glycerol backbone *
· Simple triglycerides have three identical fatty acids while mixed triglycerides have 2 or 3
different fatty acids *
· Major dietary lipid in humans and major energy store
· Synthesised from glycerol-3-phosphate (glycolytic intermediate) and fatty acyl CoA
· Fatty acids removed from triglycerides by the action of lipase and the free fatty acids
degraded by beta-oxidation
· Glucagon, adrenaline and noradrenaline increase plasma free fatty acid concentration
while insulin has the opposite effect *
· May accumulate in the liver (fatty liver) *
Question 31 Triglycerides are composed of

Three identical fatty acid chains esterified to a Three fatty acid chains esterified to a galactose
A B
glycerol backbone backbone
Three fatty acid chains esterified to a glycerol Three glycerol molecules esterified to a fatty acid
C D
backbone chain
Three galactose molecules esterified to a fatty
E
acid chain
Explanation
Question 32 Lipoproteins

A Contain triglycerides but not phospholipids B Do not contain apoproteins
C Have a hydrophilic core D Include chylomicrons
E Do not contain cholesterol

Explanation
LIPOPROTEINS *****
· Globular particles consisting of a hydrophobic core and a hydrophilic surface. Contain

triglycerides, cholesterol, phospholipids, apoproteins
· Chylomicrons carry triglycerides from the intestines to the liver, skeletal muscle and
adipose tissue.
· Very-low-density lipoproteins (VLDL) carry (newly synthesised) triglycerides from the liver
to adipose tissue.
· Intermediate-density lipoproteins (IDL) are intermediate between VLDL and LDL. They
are not usually detectable in the blood when fasting.
· Low-density lipoproteins (LDL) carry 3,000 to 6,000 fat molecules (phospholipids,
cholesterol, triglycerides, etc.) around the body. LDL particles are sometimes referred to as
"bad" lipoprotein because concentrations, dose related, correlate with atherosclerosis
progression.
· High-density lipoproteins (HDL) collect fat molecules (phospholipids, cholesterol,
triglycerides, etc.) from the body's cells/tissues, and take it back to the liver. HDLs are
sometimes referred to as "good" lipoprotein because higher concentrations correlate with low
rates of atherosclerosis progression and/or regression
Question 33 Chylomicrons

A Are synthesised by the liver B Are synthesised in the portal circulation
C Transport cholesterol from the liver D Transport dietary lipids to tissues
E Are not present in the peripheral circulation
Explanation
Chylomicrons *****
· Largest of the lipoproteins
· Synthesized by the gut and transport dietary lipids to tissues via peripheral circulation. *
· Transport cholesterol to the liver *
· Have a molecular mass of ~ 400kDa with a density of <0.95g/ml *
· Protein content is 1.5 - 2.5%
· Major lipid is triglycerides *
· At tissues, the triglycerides are hydrolysed by lipoprotein lipase

Question 34 Chylomicrons

A Are the smallest types of lipoprotein B Are the most dense lipoprotein
C Have a mass of about 400kDa D Have a protein content of 15-20%
E Have a density of about 0.095 g/ml
Explanation
Question 35 Very low density lipoprotein (VLDL)

Is converted to HDL as triglycerides are
A B Does not contain phospholipids
hydrolysed
C Is converted to IDL and then LDL D Is synthesised from LDL
E Transports cholesterol from the tissues to the liver
Explanation
VLDL *****
· Synthesized in the liver and transports lipids from the liver to other tissues.
· Molecular weight ~10-80kDa with a density of <1.006g/ml *
· Protein content 5-10%
· Contain triglycerides, phospholipids and cholesterol ester *
· Triglycerides are hydrolysed by lipoprotein lipase. As triglycerides are removed and
cholesterol is esterified with the loss of apoproteins order than apoB-100, VLDL is converted to
IDL and then to LDL
Question 36 The density of LDL is around

A 0.01 g/ml B 0.05 g/ml
C 0.1 g/ml D 0.5 g/ml
E 1.0 g/ml
Explanation
LDL *****

· Carry 3,000 to 6,000 fat molecules (phospholipids, cholesterol, triglycerides, etc.) around
the body. LDL particles are sometimes referred to as "bad" lipoprotein because concentrations,
dose related, correlate with atherosclerosis progression.
· Binds to LDL receptor * and is internalised by receptor mediated endocytosis. Cholesterol
is released by the action of lysosomal lipase.
· Molecular weight ~2.3kDa, density 1.019 - 1.063g/ml
· Protein content 20-25% *
· Major lipids are cholesterol ester and phospholipids *
· High intracellular cholesterol concentrations reduce the expression of the LDL receptor
and inhibit cellular biosynthesis of cholesterol from acetate *
Question 37 Glycogen

Is an oligosaccharide containing glucose and Is a branched chain polysaccharide containing
A B
galactose glucose
Is a polysaccharide containing glucose and
C D Is not stored in skeletal muscle
galactose
Is a branched chain polysaccharide containing
E
glucose and lactose
Explanation
GLYCOGEN
 Branched chain polysaccharide containing glucose residues *
 Stored mainly in the liver and skeletal muscle - muscle glycogen provides energy for prolonged
muscle contraction while liver glycogen is used to maintain blood glucose levels *
 Glycogen is stored in granules in the cytosol *
Question 38 During glycogenolysis, phosphorylase removes

Glucose units up to 4 residues from a branch
A All glucose units B
point
Glucose units up to 3 residues from a branch Glucose units up to 2 residues from a branch
C D
point point
E Glucose units up to the branch point
Explanation
GLYCOGENOLYSIS
 Phosphorylase catalyses the removal of glucose units by the phosphorylysis of alpha 1,4
glycosidic bonds up to 4 residues away from a branch point with the release of glucose-1
phosphate *
 Glucose-1-phosphate is converted to glucose-6-phosphate by phosphoglucomutase and this
can then enter glycolysis *

 The liver, intestines and kidneys have glucose-6-phosphatase which can release glucose from
glucose-6-phosphate. Glycogen in skeletal muscle cannot be converted into glucose as
glucose-6-phosphate cannot leave cells *
 The three residues leading up to a branch point on glycogen are transferred to another part of
the molecule by transferase
 Alpha-1,6-glycosidic bonds at branch points are cleaved by alpha-1,6 glucosidase
Question 39 Which reaction is catalysed by the enzyme glycogen synthase?

Addition of glucose units from glucose-1-
A Removal of glucose units from glycogen B
phosphate to glycogen
Addition of glucose units from glucose-6- Addition of glucose units from UDP-glucose to
C D
phosphate to glycogen glycogen
Addition of glucose units from UMP-glucose to
E
glycogen
Explanation
GLYCOGEN SYNTHESIS
 Glucose must initially be activated by conversion to UDP-glucose (Uridine diphosphate-glucose)
 Glycogen synthase catalyses the addition of glucose from UDP-glucose to the non-reducing end
of the glycogen chain, forming alpha-1,4-glycosidic bonds. Glucose residues can only be added
to a chain of five or more residues
 When the chain contains over 11 residues, a branching enzyme transfers seven residues to an
interior site, forming a branch point which must be at least four residues from any pre-existing
branch points

Glycogen metabolism is partly regulated by the activity of phosphorylase
Question 40
and glycogen synthase
Phosphorylase exists as an active (beta) form and The phosphorylated form of phosphorylase is
A B
an inactive (delta) form inactive
The phosphorylated form of glycogen synthase is The de-phosphorylated form of phosphorylase is
C D
inactive active
The phosphorylated form of glycogen synthase is
E
active
Explanation
REGULATION OF GLYCOGEN METABOLISM
form

active 'a' form

A Adrenalin inhibits glycogenolysis B Adrenalin stimulates glycogen synthesis
Adrenalin stimulates the phosphorylation of
C D Adrenalin activates protein phosphatase I
phosphorylase b
Adrenaline stimulates the phosphorylation of
E
Explanation

Explanation
GLYCOLYSIS *****
 Occurs in the cytoplasm and does not require oxygen. Principal energy generating mechanism
in the absence of oxygen of in cells such as RBC which do not have mitochondria *
 Initial reactions involve two phosphorylation steps: initially by hexokinase to form glucose-6-
phosphate (converted to fructose-6-phosphate by isomerase) and then to fructose 1,6
bisphosphate by phosphofructokinase with the hydrolysis of ATP to ADP


Question 43 How many molecules of ATP are generated per glucose molecule during glycolysis?

A One B Two
C Three D Four
E Two or three depending on oxygen levels
Explanation

A Free fatty acids B Oxaloacetate
C Lactate D Pyruvate
E Glycerol
Explanation
Question 45 Glycolysis and gluconeogenesis have to be regulated.

Gluconeogenesis is inhibited by high levels of
A Glycolysis is stimulated by high levels of ATP B
ATP
C Alanine inhibits glycolysis D Alanine inhibits gluconeogenesis
Glycogen synthase is the main enzyme that
E
regulated glycolysis
Explanation
Question 46 The following inhibit glycolysis

A High levels of ATP and low levels of alanine B High levels of alanine and low levels of ATP

C High levels of ADP and low levels of alanine D Low levels of ADP and high levels of alanine
E High levels of ATP and high levels of alanine
Explanation
Question 47 During the Cori cycle

Pyruvate is converted to glucose in skeletal
A B Pyruvate is converted to lactic acid by the liver
muscle
C NAD+ is converted to NADH in skeletal muscle D Lactate is converted to glucose by the liver
E Glucose is converted to lactate by the liver
Explanation
CORI CYCLE
 Occurs during strenuous exercise - NADH formation by glycolysis exceeds the capacity of the
respiratory chain to oxidise it back into NAD+
 Pyruvate is produce by glycolysis in skeletal muscle and converted into lactate by lactate
dehydrogenase with the NADH to NAD+, allowing glycolysis to continue to provide ATP
 Lactate diffuses out of skeletal muscle into blood, is taken up by the liver and converted into
glucose by gluconeogenesis
 Hepatic glucose is then utilised by muscle for glycolysis
Question 48 The breakdown of triglycerides occurs in

A The cytoplasm B The lysosomes
Explanation
BREAKDOWN OF TRIGLYCERIDES
 Occurs in the cytoplasm
 Mediated by hormone sensitive lipase which is activated by glucagon, adrenaline, noradrenaline
and ACTH through phosphorylation
 Insulin causes dephosphorylation and inactivation of hormone sensitive lipase

 Triglycerides are converted to one molecule of glycerol and three fatty acids
 Glycerol can enter glycolysis through phosphorylation to glycerol-3-phosphate
Question 49 Fatty acid oxidation

A Occurs exclusively in the cytoplasm B Occurs exclusively in the mitochondria
Begins in the cytoplasm and continues in the Begins in the mitochondria and continues in the
C D
mitochondria cytoplasm
E Results in the production of glycerol
Explanation
FATTY ACID OXIDATION
 Begins in the cytoplasm by the conversion of fatty acids to fatty Acyl CoA - ATP is hydrolysed to
AMP + 2Pi and CoA is required. The reaction is catalysed by Acyl CoA synthetase *
 Fatty Acyl CoA is carried into the mitochondria for beta-oxidation.* This shuttling requires the
presence of carnitine. Acyl Carnitine is formed in the cytosol, carried into the mitochondria then
converted to carnitine + Acyl CoA
 In addition to ATP, NADH and FADH2 are also produced during beta-oxidation
causing ketonuria *
Question 50 Ketone bodies

A Are fat-soluble B Cannot be excreted in the breath
C Can be used by the brain for fuel D Cannot be used by skeletal muscle for fuel
E Are mainly produced by the brain
Explanation


hydroxybutyrate
hydroxybutyrate
Explanation
Question 52 In the post-absorptive phase of starvation

A Glycogen synthase is activated B Phosphorylase is activated
There is de-phosphorylation of key enzymes
C D Hormone-sensitive lipase is inactivated
involved in carbohydrate metabolism
E Glucose is absorbed from the blood into the liver
Explanation
STARVATION
POST-ABSORPTIVE PHASE
· Insulin concentrations fall while glucagon concentrations rise *
· Phosphorylation of enzymes occurs: Glycogen synthase -inactivated, glycogen
phosphorylase - activated, hormone sensitive lipase - activated *
· Triglyceride breakdown is stimulated in adipose tissue and glycogenolysis is stimulated
with the release of glucose and fatty acids into blood. *
Question 53 The following enzymes are activated in the post-absorptive phase of starvation

A Phosphorylase and glycogen synthase B Glycogen synthase and hormone-sensitive lipase
C Phosphorylase and hormone-sensitive lipase D Phosphorylase only
E Hormone-sensitive lipase only
Explanation

Question 54 During the gluconeogenic phase of starvation
The activity of fructose-1,6-bisphoaphatase is

A B The activity of phosphofructokinase is increased
increased
C Glucose is converted to amino acids by the liver D Insulin concentrations increase
E The brain begins to use free fattu acids as fuel
Explanation
GLUCONEOGENIC PHASE
· Glycolysis is inhibited by the phosphorylation and inactivation of phosphofroctokinase and
increased activity of fructose-1,6-bisphosphatase
· Fatty acid oxidation is increased in the liver
· Amino acids are released from skeletal muscle and utilised by the liver for
gluconeogenesis
Question 55 The pentose phosphate pathway

Has a phosphorylated and a de-phosphorylated
A B Has an oxidative and a non-oxidative pathway
pathway
Has an alpha-glycolytic and a beta-glycolytic
C Has a cytosolic and a mitochondrial component D
pathway
E Occurs in the nucleus
Explanation
PENTOSE PHOSPHATE PATHWAY
· Occurs in the cytoplasm
· Starting substrate is glucose-6-phosphate
· Oxidative pathway results in the conversion of glucose-6-phosphate to ribolose-5-
phosphate with the production of NADPH
· Ribolose-5-phosphate is converted to Ribose-5-phosphate which is a precursor for DNA,
RNA, ATP, NAD+, FAD and CoA synthesis *
· Non-oxidative pathway results in the conversion of three molecules of ribolose-5-
phosphate to 2 molecules of fructose-6-phosphate and one molecule of glyceraldehyde-3-
phosphate. These can then enter the glycolytic pathway
Question 56 The citric acid (tri-carboxylic acid) cycle

Resulta in the oxidation of glucose to CO2 and
A B Cannot utilise acetyl CoA
water
C Begins in the cytosol D Occurs in mitochondria
E Can occur under anaerobic conditions

Explanation
CITRIC ACID (TRI-CARBOXYLIC ACID) CYCLE
 Oxidation of pyruvate (derived from glycolysis) to carbon dioxide and water
 Also oxidises acetyl CoA from fatty acid breakdown and amino acid degradation products
 Occurs within the mitochondria under aerobic conditions *
How many turns of the citric (tri-carboxylic) acid cycle does it take to
Question 57
completely oxidise one glucose molecule?

A One B Two
C Three D Four
E Five
Explanation
During the citric acid cycle, how many molecules of CO2 are produced per
Question 58
molecule of acetyl CoA?

A 1 B 2
C 3 D 4
E 5
Explanation
 Two molecules of CO2 are produced per molecule of acetyl CoA *
 The citric acid cycle will operate to a reduced extent unless new oxaloacetate is formed,
because acetyl CoA cannot enter the cycle unless it condenses with oxaloacetate
 Oxaloacetate is formed by the carboxylation of pyruvate, in a reaction catalyzed by the biotin-
dependent enzyme pyruvate carboxylase
 The disruption of pyruvate metabolism is the cause of beriberi secondary to thiamine deficient -
Thiamine pyrophosphate is the prosthetic group of three important enzymes: pyruvate
dehydrogenase, a-ketoglutarate dehydrogenase, and transketolase *
 The low transketolase activity of red cells in beriberi is an easily measured and reliable
diagnostic indicator of the disease
 The citric acid cycle also produces intermediates for other biosynthetic pathways.

ENZYMES & DIGESTION
Histones are integral to the structure of the chromosome. Which one is
Question 1
the linker histone(s)

A H2A B H2B and H3
E H1 and H5
Explanation
The DNA in chromosomes is associated with several proteins, of which histones are the most
abundant
histone H1/5 giving a -beads on a string- appearance

A 10 : 1 B 5:1
C 2:1 D 1:1
E 0.1 : 1
Explanation


Explanation
MESSENGER RNA
cytoplasm *
Question 4 Transfer RNA makes up

A 5% of total cellular RNA B 15% of total cellular RNA
C 35% of total cellular RNA D 55% of total cellular RNA
E 85% of total cellular RNA
Explanation
TRANSFER RNA
· Makes up 15% of total RNA

· Binds specific amino acids and carries them to the polyribosomes for protein synthesis
· There is a specific tRNA for each amino acid but some amino acids are recognised by
more than one specific tRNA and therefore have more than one codon *
· Has a clover-leaf secondary structure with an amino acid binding site at the 3- end and an
anticodon site on one of the clover leaves. The anticodon recognises the triplet codon on mRNA
*

Explanation

Question 6
residues are

C Valine D Proline
E Hydroxy-proline
Explanation

residues
residues
Cross-linking between cysteine and methionine
E
residues
Explanation

Question 8 Which one is the predominant type of collagen found in basement membranes?

A Type I B Type II
C Type III D Type IV
E Type V
Explanation
Collagen type I: two identical and one different alpha chain. Makes up 90% of total collagen and
is found in skin, bone, tendon *

E Termination
Explanation
PROTEIN SYNTHESIS
Proteins are synthesised from amino acids using the genetic code. Each
Question 10
codon is made up of

A 2 bases B 3 bases
E 3 base pairs
Explanation


Question 11 Aminoacyl tRNA synthetase plays a key role in protein synthesis.

A There are 5 different enzymes B The reaction catalysed results in ATP production
The reaction catalysed results in the formation of
C There are 20 different enzymes D
disulphide bonds
There are 3 different enzymes – alpha, beta and
E
gamma
Explanation
Question 12 During protein synthesis, the start codon is

A TTT B GAU
C AUG or GAU D AUG
E AUG or TTT
Explanation
INITIATION - Protein synthesis begins when the ribosomal subunits come together with the
mRNA molecule and the initiator tRNA molecule carrying the amino acid METHIONINE *
The start codon is AUG and the first amino acid to be added is always METHIONINE. This is
usually excised during post-translational modification
There are two sites on the ribosome - the P (Peptidyl) site occupied by the peptide chain and
the A (aminoacyl) site to which new aminoacyl-tRNA molecules are added
Question 13 Which one is not an example of post-translational modification of proteins?

A Glycosylation B Disulphide bond formation
C Peptide bond formation D Proteolysis
E Hydroxylation

Explanation
POST-TRANSLATIONAL MODIFICATIONS *****
• Excision of signal sequences - these sequences target proteins to specific sites,
mitochondria for instance and are removed once the target is reached. Nuclear proteins have
arginine and lysine -rich sequences
• Disulphide bond formation
• Proteolysis - for instance the conversion of pro-hormones to hormones
• Glycosylation - three types: N-linked; O-linked and addition of the glycosyl
phosphatidylinositol anchor to membrane proteins
• O-linked glycosylation occurs by the sequential addition of monosaccharide units to the
OH group of serine or threonine sidechains
• N-linked glycosylation is the addition of oligosaccharide molecules to the NH2 groups of
asparagine sidechains
• Proteins may be modified during translation - for instance proline is hydroxylated during
collagen synthesis

A Uric acid B Urea
E Acetate
Explanation
UREA *****
urea cycle
kidneys

E
phosphorylase b

Explanation
form
active 'a' form
Question 16 Ketone bodies are produced when

The rate of fatty acid oxidation exceeds oxygen
A The rate of glycolysis exceeds oxygen availability B
availability
The rate of fatty acid oxidation exceeds the rate of The rate of carbohydrate breakdown exceeds the
C D
glycerol synthesis rate of protein synthesis
The rate of fatty acid oxidation exceeds the rate of
E
carbohydrate breakdown
Explanation

causing ketonuria *

hydroxybutyrate
hydroxybutyrate
Explanation
Question 18 The fetal brain

A Can utilise ketone bodies as fuel B Only utilises glucose as fuel
C Can utilise glucose and ketone bodies as fuel D Only utilises ketone bodies as fuel
Can utilise ketone bodies as fuel if the woman
E
has type 1 diabetes
Explanation
Question 19 The pentose phosphate pathway occurs in

A The nucleus B The mitochondria
C The mitochondria and cytoplasm D The lysosomes
E The cytoplasm
Explanation
PENTOSE PHOSPHATE PATHWAY
· Occurs in the cytoplasm
· Starting substrate is glucose-6-phosphate
· Oxidative pathway results in the conversion of glucose-6-phosphate to ribolose-5-
phosphate with the production of NADPH

· Ribolose-5-phosphate is converted to Ribose-5-phosphate which is a precursor for DNA,
RNA, ATP, NAD+, FAD and CoA synthesis *
· Non-oxidative pathway results in the conversion of three molecules of ribolose-5-
phosphate to 2 molecules of fructose-6-phosphate and one molecule of glyceraldehyde-3-
phosphate. These can then enter the glycolytic pathway
Question 20 The starting product for the citric (tri-carboxylic) acid cycle is

A Glucose B Citrate
C Pyruvate D Glucose-6-phosphate
E Acetyl CoA
Explanation
CITRIC ACID (TRI-CARBOXYLIC ACID) CYCLE
 Glycolysis breaks 1 glucose into 2 pyruvate, producing 6 ATP.
 Pyruvate is used to make acetyl-CoA, the starting product for the citric acid cycle.

A B
Explanation
PROTEIN DIGESTION
STOMACH


Question 22 With respect to the properties of enzymes, a cofactor is

A molecule that increases the rate at which
A A molecule that increases the rate of the reaction B
equilibrium is reached
A molecule that modifies the activity of the
C D A molecule that alters the product of the reaction
enzyme
A molecule that reduces the rate at which
E
equilibrium is reached
Explanation
PROPERTIES OF ENZYMES *****
 Proteins which catalyse chemical reactions but are unchanged at the end of the reaction
 Increase the rate at which equilibrium is reached but do not alter the direction of the reaction or
the equilibrium constant
 Reduce the activation energy required for the reaction
 Have an optimum pH for their action - pH affects enzyme structure, degree of ionisation of
substrate and enzyme-substrate interaction *
 Rate of enzyme catalysed reaction increases with increased temperature but above 40C, the
enzyme becomes progressively inactivated *
 Enzymes are specific for specific substrates and for the reaction catalysed. They have an active
site which undergoes a conformational change on contact with substrate to accommodate the
substrate (induced fit model). The enzyme-substrate complex is held together by non-covalent
forces - hydrogen and hydrophobic bonds, electrostatic and van der Waals forces *
 Some enzymes are regulated by phosphorylation / dephosphorylation
Activity of some enzymes is modified by the presence of co-factors *
During chemical reactions catalysed by enzymes, the enzyme-substrate

Question 23
complex is held together by
A Hydrogen and di-sulphide bonds B Covalent bonds and van der Waals forces
C Hydrophobic and di-sulphide bonds D Hydrogen and hydrophobic bonds
E Covalent and hydrogen bonds
Explanation
Question 24 Which one is not a recognised property of enzymes?

A Are inactivated at temperatures over 40 C B Are inactivated by de-phosphorylation
C Have an optimum pH for their action D Do not alter the equilibrium constant for a reaction
E Are specific for specific substrates

Explanation
Question 25 The velocity of an enzyme reaction

For a given concentration of enzyme, is
A Is lowest at time t = 0 B
proportional to the substrate concentration
C Is highest at time t = 0 D Is independent of the substrate concentration
E Is independent of the concentration of product
Explanation
ENZYME KINETICS
 VELOCITY: The rate of an enzyme-catalysed reaction. Highest at time t=0 (initial velocity, V0)
because the substrate concentration is maximum and there is no product formed (product may
have feed-back inhibition on enzyme activity)
 If the substrate concentration is progressively increased for a fixed enzyme concentration, there
comes a point where all the active sites on the enzyme are occupied and the initial velocity of
the reaction cannot be increased further. This is the maximum velocity Vmax
 If there is an excess of substrate, the initial velocity is proportional to the enzyme concentration
and vice-versa
 The initial velocity is given by the Michaelis-Menten equation:
V0 = (Vmax[S]) /([S] +Km): Km = Michaelis constant which is the substrate concentration at

which the initial velocity of the reaction is half the maximum velocity
With respect to enzyme kinetics, when there is an excess amount of

Question 26
substrate, the initial velocity of the reaction is

A Equal to the Michaelis constant B Proportional to the substrate concentration
C Proportional to the product concentration D Proportional to the enzyme concentration
E Equal to the square root of the Michaelis constant
Explanation

Question 27 With respect to enzyme kinetics, the Michaelis constant is

A B The initial velocity at t = 0.5
C D velocity is proportional to the substrate
concentration
E
velocity is equal to Vmax
Explanation
Question 28 With respect to enzyme kinetics, the Michaelis constant Km

Is a measure of the affinity of the enzyme for its
A Is a measure of enzyme activity B
substrate
Is higher for enzymes with high affinity for their
C D Is the same for every enzyme
substrate
E Is a measure of the Vmax
Explanation
 The Km is a measure of the affinity of the enzyme for its substrate - the higher the Km, the lower
the affinity
 The plot of initial velocity against substrate concentration gives a rectangular hyperbole. There
are various methods of deriving a linear equation from the Michaelis-Menten equation. One of
these, the Lineweaver-Burk plot used a plot of 1/V0 against 1/[S]. The intercept on the y-axis =
1/Vmax and the slope of the line = Km/Vmax
 The SI unit of enzyme activity is the katal (kat) = the quantity of enzyme in the presence of
which one mole of substrate is converted to product in one second under optimal conditions for
the activity of that enzyme
 The standard unit of enzyme activity U is the amount of enzyme catalysing the conversion of 1
micromol of substrate per minute under optimal conditions for the activity of that enzyme
Question 29 The Lineweaver-Burk plot

A Is a rectangular hyperbola B Is linear
Is a logarithmic transformation of the Michaelis-
C D Has a slope which = Km
Menten equation
E Has an intercept on the y-axis at Vmax

Explanation
Question 30 The SI unit for enzyme activity is

A Svedberg units B MicroM per second
C Katal D Michaelis units
E Kilo Joules
Explanation

Question 31 With respect to enzyme kinetics, a graph plotting 1/V0 against 1/[S] is

A A rectangular hyperbola B The Michaelis-Menten plot
C The Lineweaver-Burk plot D Intercepts the x-axis at Vmax
E Has a slopw = Km
Explanation
Question 32 With respect to the different types of enzyme inhibitors

A Reversible inhibition is always competitive B Non-competitive inhibition is always irreversible
Irreversible inhibitors bind to enzymes by non- Reversible inhibitors bind to enzymes by covalent
C D
covalent forces forces
Reversible inhibitors can be competitive or non-
E
competitive
Explanation
ENZYME INHIBITORS

Can reversible or irreversible. Reversible inhibition can be competitive or non-competitive
IRREVERSIBLE INHIBITION *-permanent enzyme inhibition usually due to covalent
binding of the inhibitor to the enzyme
REVERSIBLE INHIBITION - bind non-covalently to the enzyme and can be removed by

dialysis
The activity of enzymes can be influenced by competitive inhibitors.

Question 33
Competitive inhibitors
Cause an apparent increase in the Km of the

A B Cannot be converted to product by the enzyme
enzyme
C Cause a reduction in the Vmax of the enzyme D Result in the Km of the enzyme being unchanged
Can result in an apparent increase in the Vmax of
E
the enzyme
Explanation
Question 34 With respect to competitive and non-competitive enzyme inhibitors
Competitive inhibitors reduce the Km and the Non-competitive inhibitors reduce the Km but the
A B
Vmax of the enzyme Vmax is unchanged
Both competitive and non-competitive inhibitors Both competitive and non-competitive inhibitors
C D
increase the Km reduce the Vmax
Non-competitive inhibitors reduce the Vmax but
E
competitive inhibitors do not alter the Vmax
Explanation

NON-COMPETITIVE INHIBITION
binds to the enzyme at a site other than the active site. The substrate may still bind to
the enzyme but is not converted to product. Enzyme is effectively removed from the
reaction. The Km is unchanged but the Vmax is reduced, hence the y-intercept and the
slope of the Lineweaver-Burk plot are both altered.
Question 35 Allosteric enzymes

Are enzymes that can catalyse reactions involving
A Are enzymes that have L- and D- isomers B
more than one substrate
Are enzymes who activity is altered by ligand Can be activated or inhibited by ligand binding to
C D
binding to the substrate-binding site non-substrate binding sites
E Are enzymes that do not show a Vmax
Explanation
ALLOSTERIC ENZYMES
 Enzymes whose activity is altered by the binding of ligands to sites other than the substrate
binding site. Ligand binding may result in activation or inhibition of enzyme activity. Ligands are
allosteric activators or inhibitors *
 K-class: ligand binding results in ALTERED Km but no change in Vmax (see competitive
inhibition). Lineweaver-Burk plot: y-intercept unchanged but slope is changed
 V-class: ligand binding results in ALTERED Vmax but unchanged Km (see non-competitive
inhibition). Lineweaver-Burk plot shows altered y-intercept and slope
 If the enzyme is an oligomer (more than one identical subunits), the individual units are known
as protomers. Homotropic interaction is when an allosteric ligand increases the affinity of
another protomer for the same ligand. The interaction is heterotropic if the affinity for a different
ligand is increased.
Question 36 Enzyme cofactors

Bind to enzymes and convert them to apo-
A Are proteins or polypeptides B
enzymes
Are always bound to the enzyme by covalent
C Can be co-enzymes or prosthetic groups D
bonds
Are always bound to the enzyme by non-covalent
E
bonds
Explanation
COFACTORS
 Non-protein molecules that are necessary for enzyme action. Two main groups

 COENZYMES -may be metal ions such as Mn2+ or Zn2+ or or complex organic molecules such
as NAD+, NADP+, FAD and Flavine mononucleotide (FMN) - they are non-covalently bound to
the enzyme
 PROSTHETIC GROUPS -are covalently bound to the enzyme at its active site and include
metal ions and organic molecules such as biotin
The protein part of the enzyme without its cofactor is called an apoenzyme
Question 37 Which one is a recognised co-enzyme?

A Mn2+ B NAD+
C NADP+ D Zn2+
E All the above
Explanation
Question 38 Enzyme prosthetic groups

A Increase the Vmax of the enzyme B Reduce the Km of the enzyme
C Bind to the enzyme by covalent bonds D Convert the enzyme into an apo-enzyme
E Are types of co-enzyme
Explanation
Question 39 Which one is not a recognised mechanism of enzyme regulation in vivo?
A Inactivation of enzymes by covalent modification B Inactivation of enzymes by phosphorylation

C Activation of enzymes by phosphorylation D Activation of enzymes by proteolysis
E Inhibition of enzyme activity by allosteric groups
Explanation
REGULATION OF ENZYME ACTIVITY IN VIVO
 Regulation of enzyme protein synthesis - the total amount of enzyme present is a balance
between synthesis and degradation

 Feed-back inhibition - end-product often feeds back to inhibit the committed step earlier on in
the same pathway
 Allosteric modification - enzyme activity altered by the binding of allosteric activators / inhibitors
 Reversible covalent modification - most commonly phosphorylation / dephosphorylation
 Proteolytic activation - digestive enzymes / coagulation pathway
 Enzymes are not activated by the products of their reaction otherwise a vicious cycle would
develop. Irreversible covalent modification does not regulate enzyme activity in vivo but is the
mechanism of action of drugs / toxins
Question 40 In the stomach, hydrochloric acid is produced by

A Chief cells B Oxyntic cells
C Myoepithelial cells D Crypt cells
E Mucosal cells
Explanation
PROTEIN DIGESTION
STOMACH
Question 41 The optimal pH for the action of pepsin is
A 1-2 B 2-3
C 3-4 D 4-5
E 5-6
Explanation


A B
Explanation
PROTEIN DIGESTION
STOMACH

Explanation
SMALL INTESTINE
· Enterokinase - secreted by duodenal mucosa: proteolytic conversion of trypsinogen to
trypsin
· Bicarbonate secreted by the pancreas and biliary tree provides the optimal pH for enzyme
action
· Trypsin also activates trypsinogen in addition to other zymogens including
chymotrypsinogen, pro-elastase and pro-carboxypeptidase
polypeptide chain
· Carboxypeptidases release amino acids from the carboxy terminal of the polypeptide
chain
· Endopeptidases, aminopeptidases and dipeptidases are present in the brush-border of
intestinal epithelial cells and hydrolyse oligopeptides
· Amino acids, dipeptides and tripeptides are absorbed. Further breakdown of di- and tri-
peptides occurs within intestinal epithelial cells

A Pepsin B Trypsin
E Enterokinase
Explanation
Question 45 Salivary amylase
A Hydrolyses peptide bonds B Converts pepsinogen to pepsin

Hydrolyses triglycerides to free fatty acids and
C Hydrolyses glycosidic bonds D
glycerol
E Is most active in an acidic environment
Explanation
ARBOHYDRATE DIGESTION *****
MOUTH
· Salivary amylase is inactivated by the acidic environment in the stomach. Enzymatic
digestion of carbohydrates does not occur in the stomach
· Pancreatic amylase is secreted by the pancreas and continues the hydrolysis of glycosidic
bonds. Bicarbonate provides optimal pH for enzyme action
· Ologosaccharides and disaccharides are further digested by enzymes within the brush
border of intestinal epithelial cells: Sucrase: sucrose to glucose + fructose; Lactase: Lactose to
glucose + galactose; Maltase: maltose to glucose
· Lactase deficiency results in impaired lactose digestion. Lactose is fermented by bacteria
in the colon producing gas and osmotically active products which cause flatulence and
diarrhoea
Question 46 Enzymatic digestion of carbohydrates

Occurs in the mouth, stomach and small
A B Occurs in the stomach and small intestines only
intestines
C Does not occur in the stomach D Is undertaken by amylase and pepsin
E Is undertaken by pepsinogen and trypsinogen
Explanation

CARBOHYDRATE DIGESTION *****
MOUTH
· Salivary amylase is inactivated by the acidic environment in the stomach. Enzymatic
digestion of carbohydrates does not occur in the stomach
· Pancreatic amylase is secreted by the pancreas and continues the hydrolysis of glycosidic
bonds. Bicarbonate provides optimal pH for enzyme action
· Ologosaccharides and disaccharides are further digested by enzymes within the brush
border of intestinal epithelial cells: Sucrase: sucrose to glucose + fructose; Lactase: Lactose to
glucose + galactose; Maltase: maltose to glucose
· Lactase deficiency results in impaired lactose digestion. Lactose is fermented by bacteria
in the colon producing gas and osmotically active products which cause flatulence and
diarrhoea
Question 47 During the digestion of carbohydrates
Sucrase converts sucrose to glucose and

A B Lactase converts lactose to glucose and fructose
galactose
C Maltase converts maltose to glucose and fructose D Sucrase converts sucrose to glucose and fructose
Maltase converts maltose to glucose and
E
galactose
Explanation
Question 48 The digestion of lipids

A Begins in the mouth B Does not occur in the stomach
C Is undertaken by amylase and lipase D Occurs in the mouth and stomach
E Begins in the stomach
Explanation
LIPID DIGESTION
· Begins in the stomach by the action of lingual lipase secreted by glands at the back of the
tongue and active in the acidic pH of the stomach. Hydrolyses triglycerides to fatty acids, mono -
/ di-acylglycerol and glycerol *
· Main enzymatic digestion of fats occurs in the small intestine
· Pancreas secretes pancreatic lipase, lipid esterase and phospholipase A2 with
bicarbonate providing the optimal pH for enzyme action. Pancreatic lipase is inhibited by bile
acids but activated by colipase -secreted by the pancreas as procolipase and activated by
trypsin. Lipid esterase and phospholipase A2 require bile acids for optimal function
N = 27

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This Copy is for Dr.

Question 1 With respect to the structure of nucleic acids

Question 2 With respect to the structure of nucleic acids

Question 3 Nucleic acids are formed from

This Copy is for Dr. Mohamed ElHodiby

Question 5 To form nucleosomes, DNA is wrapped around

This Copy is for Dr. Mohamed ElHodiby

Question 9 In a chromosome, the ratio of DNA to histones on a weight basis is

Question 10 Messenger RNA (mRNA)

This Copy is for Dr. Mohamed ElHodiby

Question 11 Svedberg units

Question 12 Mature messenger RNA

This Copy is for Dr. Mohamed ElHodiby

· Makes up 80% of total cellular RNA *

Question 14 With respect to the differences between mRNA and rRNA

Question 15 With respect to transfer RNA

This Copy is for Dr. Mohamed ElHodiby

This Copy is for Dr. Mohamed ElHodiby

Question 19 Messenger RNA is synthesized by

Question 20 Post-transcriptional mRNA processing includes

This Copy is for Dr. Mohamed ElHodiby

Question 22 During the cell cycle, DNA synthesis occurs

A In the S and M phases B In the S, G1 and G2 phases

Question 23 During DNA replication

This Copy is for Dr. Mohamed ElHodiby

Question 24 With respect to the action of DNA polymerases

Rapidly dividing (malignant) cells are most sensitive to anti-metabolite chemotherapy

This Copy is for Dr. Mohamed ElHodiby

A Western blotting B Northern blotting

A DNA ligase B DNA helicase

This Copy is for Dr. Mohamed ElHodiby

Question 29 Vectors are

This Copy is for Dr. Mohamed ElHodiby

This Copy is for Dr. Mohamed ElHodiby

Question 34 In the human adult, uric acid levels

This Copy is for Dr. Mohamed ElHodiby

Low uric acid concentration *****

Question 36 With respect to renal handling of urea

This Copy is for Dr. Mohamed ElHodiby

A The glomerulus B The proximal convoluted tubule

Question 38 With respect to renal excretion of urea, carrier-mediated reabsorption occurs in

Question 39 Urea reabsorption in the medullary collecting ducts

A Is independent of anti-diuretic hormone B Increases at low urine flow rates

This Copy is for Dr. Mohamed ElHodiby

A Mainly excreted by the kidneys B Mainly synthesised from triglycerides

Question 41 Simple triglycerides have

A Three identical fatty acid chains B Three glycerol molecules

This Copy is for Dr. Mohamed ElHodiby

Question 43 With respect to the regulation of glycogen metabolism

This Copy is for Dr. Mohamed ElHodiby

Question 44 Which molecule(s) can be metabolised by glycolysis?

Glucose + 2Pi + 2ADP + 2NAD+ = 2pyruvate + 2H2O + 2ATP + 2NADH + 2H+ *

Question 45 The enzyme phosphofructokinase plays a key role in

This Copy is for Dr. Mohamed ElHodiby

Question 46 Fatty acid synthesis occurs in

Question 47 Which one inhibits the activity of hormone-sensitive lipase?

This Copy is for Dr. Mohamed ElHodiby

Question 49 Ketone bodies include

Acetic acid, acetoacetate and beta-

Question 50 In the post-absorptive phase of starvation

This Copy is for Dr. Mohamed ElHodiby

Question 51 During the ketotic phase of starvation

A Ketone bodies inhibit insulin secretion B Insulin secretion is increased