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Medical Biological Chemistry – Test Assignments (Cover pages)

Total questions: 150

Worksheet time: 1hrs 15mins

Name
Class
Date
1.

Sulfur-containing amino acids include

a)

val

b)

cis

c)

ala

d)

tyr

e)

gly

2.

The structural unit of a protein is

a)

nucleotide

b)

nucleoside

c)

amino acid

d)

purine base

e)

monosaccharide

3.

Neutral amino acids include

a)

lys

b)

arg

c)

glu

d)

ser

e)

asp

4.

Alkaline amino acids include

a)

tri

b)

lys

c)

ala

d)

met

e)

ser

5.

The primary structure of a protein is maintained by bonds

a)

hydrogen

b)

peptide

c)

hydrophobic

d)

ionic

e)

disulfide

6.

Acidic amino acids include

a)

his

b)

tre

c)

leu

d)

asp

e)

val

7.

Select the definition of the primary structure of a protein

a)

amino acid composition of the polypeptide chain

b)

linear structure of the polypeptide chain formed by covalent bonds between amino acid radicals

c)

the order of alternation of amino acids linked by peptide bonds in a protein

d)

structure of the polypeptide chain stabilized by hydrogen bonds

e)

spatial association of several chains

8.

Tertiary Protein structure is maintained by bonds

a)

disulfide

b)

hydrogen

c)

hydrophobic

d)

ionic

e)

all of the above

9.

The quaternary structure of a protein is maintained by bonds

a)

peptide

b)

disulfide

c)

hydrogen

d)

all of the above are correct

e)

only ionic

10.

Select the definition of the secondary structure of a protein

a)

the way protomers are folded in oligomeric proteins

b)

the sequence of amino acids linked by peptide bonds

c)

spatial folding of the chain due to radicals

d)

the way the polypeptide chain is folded in the form of an α-helix and β-sheet

e)

the number of protomers in Protein

11.

The secondary structure of a protein is maintained by bonds

a)

peptide

b)

hydrogen

c)

disulfide

d)

ionic

e)

hydrophobic

12.

Select the definition of tertiary protein structure

a)

a structure stabilized by hydrogen bonds in the peptide backbone

b)

a conformation of the polypeptide chain due to interactions between amino acid radicals

c)

the mode of protomer folding

d)

amino acid sequence

e)

α- and β-structures

13.

Which protein structure is genetically determined

a)

primary

b)

secondary

c)

tertiary

d)

quaternary

e)

supramolecular

14.

Select the most complete definition of quaternary protein structure

a)

the mode of polypeptide chain folding

b)

fibrillar structure

c)

the number of protomers, their arrangement, and the nature of the bonds between them

d)

the order of amino acid alternation

e)

secondary protein structure

15.

Factors that influence protein stability are

a)

water shell and charge

b)

molecular weight and IEC of the medium

c)

the presence of a prosthetic group and a cofactor

d)

all of the above are correct

e)

only temperature

16.

Which protein structure is resistant to denaturation

a)

primary

b)

secondary

c)

tertiary

d)

quaternary

e)

secondary and tertiary

17.

In the isoelectric state, proteins

a)

are most stable

b)

are highly soluble

c)

have the greatest charge

d)

are least stable

e)

are completely denatured

18.

Protein denaturation is accompanied by

a)

destruction of non-covalent bonds

b)

decreased solubility

c)

destruction of secondary, tertiary, and quaternary structures

d)

loss of biological activity

e)

all of the above

19.

Fibrillar proteins include

a)

collagen

b)

globulin

c)

hemoglobin

d)

albumin

e)

ferritin

20.

In addition to the protein component, complex proteins contain

a)

carbohydrates

b)

lipids

c)

metals

d)

heme

e)

all of the above are correct

21.

Simple proteins include

a)

chromoproteins

b)

histones

c)

lipoproteins

d)

phosphoproteins

e)

nucleoproteins

22.

Blood albumins provide

a)

oxygen transport

b)

colloid osmotic pressure

c)

immune defense

d)

nerve impulse transmission

e)

participation in blood clotting

23.

Chromoproteins include

a)

hemoglobins

b)

globulins

c)

Albumins

d)

Histones

e)

Collagen

24.

Nucleoproteins are complexes of nucleic acid and

a)

Albumin

b)

Globulin

c)

Histone

d)

Heteroglycans

e)

Collagen

25.

The predominant amino acids in the structure of collagen are

a)

Proline and hydroxyproline

b)

Serine and threonine

c)

Methionine and cysteine

d)

Phenylalanine and tyrosine

e)

Lysine and arginine

26.

Proteinoids perform the following functions

a)

Plastic

b)

Catalytic

c)

Regulatory

d)

Transport

e)

Energy

27.

The primary structure of nucleic acid is determined by bonds

a)

Peptide

b)

Disulfide

c)

Hydrogen

d)

Phosphodiester

e)

Ionic

28.

DNA performs the following functions

a)

Stores genetic information

b)

Transports various substances

c)

Catalyzes chemical reactions

d)

Energy source cells

e)

participates in ATP synthesis

29.

Nucleic acids are polymers consisting of

a)

amino acids

b)

nucleosides

c)

nucleotides

d)

purine bases

e)

proteins

30.

Messenger RNA performs the following functions

a)

transport

b)

catalytic

c)

plastic

d)

delivers information about protein structure to ribosomes

e)

participates in DNA replication

31.

The primary structure of DNA includes

a)

dAMP

b)

dGMP

c)

dCMP

d)

TMP

e)

all of the above are correct

32.

Indicate which participant in proline hydroxylation during collagen synthesis

a)

ascorbic acid

b)

aspartic acid

c)

vitamin A

d)

arginine

e)

vitamin E

33.

The primary structure of RNA includes

a)

AMP

b)

GMP

c)

CMP

d)

UMP

e)

all of the above are correct

34.

Indicate the function of heat shock proteins

a)

Regulate the excretion of electrolytes by the kidneys

b)

Participate in the folding and assembly of complex proteins

c)

Control the ornithine cycle

d)

Activate tyrosine kinase

e)

Participate in DNA replication

35.

Indicate which of the following coenzymes does not contain vitamins

a)

THF

b)

PALP

c)

ATP

d)

FMN

e)

TPP

36.

An inhibitor is similar in structure to its substrate. Name the type of inhibition

a)

Nonspecific

b)

Competitive

c)

Allosteric

d)

Noncompetitive

e)

Irreversible

37.

Indicate which of the following coenzymes contains vitamins

a)

ATP

b)

FAPS

c)

FAD

d)

glutathione

e)

creatine phosphate

38.

An inhibitor causes enzyme denaturation. Name the type of inhibition

a)

specific

b)

competitive

c)

allosteric

d)

non-specific

e)

reversible

39.

Name the principle underlying the classification of enzymes

a)

substrate loss and reaction product accumulation

b)

substrate structure

c)

type of catalyzed reaction

d)

coenzyme structure

e)

molecular weight

40.

What class of enzymes does the coenzyme NAD interact with

a)

oxidoreductases

b)

transferases

c)

hydrolases

d)

lyases

e)

isomerases

41.

Phosphopyridoxal is a coenzyme

a)

oxidoreductases

b)

transferases

c)

hydrolases

d)

isomerases

e)

lyases

42.

Specify the functions of the allosteric center

a)

Directly involved in catalysis

b)

Participates in the binding of apo- and coenzyme

c)

Binds to low-molecular-weight effectors that regulate enzyme function

d)

Binds substrate

e)

Catalyzes ATP hydrolysis

43.

Non-enzymatic antioxidants include

a)

histamine

b)

vitamin B6

c)

alanine

d)

α-tocopherol

e)

isomerases

44.

Rickets is characterized by

a)

impaired oxidative Decarboxylation of polyvinylpyrrolidone (PVK)

b)

Impaired oxidative phosphorylation

c)

Impaired calcium phosphate deposition in bone tissue

d)

Impaired methyl group transfer

e)

Impaired protein synthesis

45.

Which vitamin is a component of the coenzyme involved in hydrogen atom transfer

a)

Riboflavin

b)

Thiamine

c)

Nicotinic acid

d)

Vitamin K

e)

Biotin

46.

Indicate the reasons for changes in enzyme activity with changes in pH:

a)

The degree of dissociation of ionogenic groups changes

b)

The conformation of the enzyme molecule changes

c)

The dissociation of ionogenic groups of the substrate changes

d)

Answers a, b, c

e)

Changes in molecular weight Enzyme

47.

Indicate the main reason for the decrease in enzyme activity with increasing temperature:

a)

change in the degree of dissociation of ionogenic groups

b)

destruction of peptide bonds

c)

enzyme denaturation

d)

disruption of coenzyme function

e)

decrease in substrate concentration

48.

Trypsin cleaves bonds:

a)

glycoside

b)

peptide

c)

ester

d)

disulfide

e)

phosphodiester

49.

Name the substrates that gastric juice pepsin participates in the cleavage of:

a)

polysaccharides

b)

triglycerides

c)

proteins and peptides

d)

steroids

e)

nucleic acids

50.

Coenzymes of lyase reactions include:

a)

vitamin K

b)

NAD

c)

FAD

d)

lipoic acid

e)

TPP

51.

Enzymes by chemical nature are:

a)

carbohydrates

b)

lipids

c)

minerals

d)

proteins

e)

Nucleic acids

52.

The International Classification of Enzymes divides enzymes into six classes according to:

a)

activity

b)

structure

c)

type of catalyzed reaction

d)

substrate specificity

e)

organ affiliation

53.

Increased enzyme activity in the blood serum during pathology may be a consequence of:

a)

increased enzyme synthesis

b)

increased cell membrane permeability

c)

cytolysis

d)

answers a, b, c

e)

decreased body temperature

54.

The highest ALT activity is found in cells:

a)

liver

b)

myocardium

c)

kidneys

d)

pancreas

e)

spleen

55.

The myocardium contains the highest amount of the isoenzyme:

a)

LDH-1

b)

LDH-2

c)

LDH-3

d)

LDH-4

e)

LDH-5

56.

The rate of an enzymatic reaction depends on:

a)

temperature

b)

pH

c)

substrate concentration

d)

presence of cofactors

e)

all of the above are correct

57.

The value of the Michaelis constant reflects:

a)

the dependence of the reaction rate on temperature

b)

affinity of the enzyme and substrate

c)

the effect of coenzymes on Enzymes

d)

dependence of reaction rate on pH

e)

molecular weight of the enzyme

58.

What action does a competitive inhibitor have:

a)

binds the substrate

b)

interacts with the allosteric center

c)

denatures the apoenzyme

d)

blocks the active site

e)

destroys peptide bonds

59.

Indicate what distinguishes enzymes from inorganic catalysts:

a)

ability to accelerate reactions

b)

does not change the direction of the reaction

c)

emerges from the reaction unchanged

d)

thermolability

e)

participation in energy metabolism

60.

The optimum pH for salivary amylase is:

a)

1.5–2.0

b)

8.0–8.3

c)

6.8–7.0

d)

10.0–11.0

e)

4.5–5.0

61.

Name the enzyme that cleaves bonds in the starch molecule:

a)

chymotrypsin

b)

amylase

c)

lipase

d)

Elastase

e)

Pepsin

62.

Avidin is a protein that irreversibly binds biotin enzymes. Indicate which transformations will be disrupted by avidin:

a)

glucose → PVK

b)

PVK → OXYGEN

c)

glucose → ribose-6-phosphate

d)

glycogen → glucose

e)

lactate → PVK

63.

Indicate which enzyme is involved in the hydrolysis of triglycerides:

a)

chymotrypsin

b)

amylase

c)

lipase

d)

elastase

e)

pepsin

64.

Indicate the group of coenzymes that are vitamin derivatives:

a)

FAD, glutathione, NAD

b)

FAPS, ATP, biotin

c)

cobamide coenzyme, FMN, biotin

d)

glutathione, heme, THF

e)

creatine phosphate, ATP

65.

Indicate the vitamin deficiency for which a characteristic disorder of collagen synthesis is:

a)

xerophthalmia

b)

rickets

c)

scurvy

d)

pellagra

e)

polyneuritis

66.

Vitamin A deficiency leads to:

a)

pellagra

b)

rickets

c)

xerophthalmia

d)

polyneuritis

e)

scurvy

67.

Indicate the disease caused by a lack of vitamin PP:

a)

scurvy

b)

polyneuritis

c)

rickets

d)

xerophthalmia

e)

pellagra

68.

The prosthetic group of rhodopsin, a protein in the retina, is:

a)

calciferol

b)

tocopherol

c)

phylloquinone

d)

retinal

e)

thiamine

69.

Vitamins are compounds:

a)

exhibiting the same physical properties

b)

having the same chemical structure

c)

synthesized in any organism

d)

ensuring the functioning of enzymes in small concentrations

e)

being part of proteins

70.

Name the characteristic An enzyme with absolute specificity:

a)

catalyzes reactions with several similar substrates

b)

interacts with stereoisomers of a substrate

c)

catalyzes a single reaction

d)

participates in the conversion of a group of substrates

e)

is activated by metal ions

71.

Hypovitaminosis develops with the use of antibiotics. Indicate the cause:

a)

impaired conversion of a vitamin to a coenzyme

b)

vitamin deficiency in food

c)

impaired absorption

d)

suppression of intestinal microflora

e)

increased renal excretion of vitamins

72.

Proteolytic enzymes are used:

a)

in the treatment of malignant tumors

b)

for the removal of necrotic tissue

c)

for the treatment of rickets

d)

in the treatment of polyneuritis

e)

for vitamin deficiencies

73.

Salivary amylase catalyzes:

a)

phospholipid hydrolysis

b)

polypeptide hydrolysis

c)

starch hydrolysis

d)

neutral fat hydrolysis

e)

nucleic acid hydrolysis

74.

Select the main structural and functional features of allosteric enzymes:

a)

are oligomeric proteins

b)

have an allosteric center

c)

are "key" enzymes

d)

answers a, b, c

e)

consist of one subunit

75.

Quantitative determination of enzymes in tissues and biological fluids is used:

a)

for disease diagnosis

b)

in the preparation of enzyme preparations

c)

to monitor the effectiveness of treatment for a number of diseases

d)

answers a, b, c

e)

to determine blood type

76.

What is the basis for dividing enzymes into classes? lies in:

a)

the structure of the substrate

b)

the structure of the reaction products

c)

the structure of the coenzymes

d)

the type of catalyzed reaction

e)

the molecular weight of the enzyme

77.

The biological significance of vitamins is:

a)

they are a source of energy

b)

they are structural components of cells

c)

they are part of coenzymes

d)

they perform a regulatory function

e)

they participate in the synthesis of nucleic acids

78.

Causes of hypovitaminosis:

a)

impaired incorporation of vitamins into coenzymes

b)

vitamin deficiency in food

c)

impaired absorption of vitamins

d)

suppression of intestinal microflora

e)

all of the above are correct

79.

Functions of metals in enzymatic catalysis:

a)

they participate in the binding of the enzyme to the substrate

b)

they participate in the formation of the active site

c)

they participate in the binding of the coenzyme to the apoenzyme

d)

they stabilize the quaternary structure of the enzyme

e)

all of the above are correct

80.

Indicate the similarities between enzymes and inorganic catalysts:

a)

they act at high temperatures

b)

they are consumed during the reaction

c)

they have a high specificity

d)

bypass the energy barrier

e)

are protein in nature

81.

Isoenzymes differ from each other by:

a)

pH optimum

b)

electrophoretic mobility

c)

immunological characteristics

d)

all of the above are correct

e)

thermal stability

82.

Types of enzyme specificity:

a)

absolute

b)

relative (group)

c)

stereochemical

d)

answers a, b, c

e)

temperature

83.

Which vitamin is specific for amino acid metabolism:

a)

nicotinic acid

b)

thiamine

c)

biotin

d)

pyridoxine

e)

vitamin E

84.

General properties of enzymes include:

a)

thermolability

b)

pH optimum

c)

specificity

d)

all of the above are correct

e)

ability to work in very low concentrations

85.

Isoenzymes are:

a)

several different enzymes

b)

isomolecular forms of a single enzyme

c)

multienzyme complexes

d)

enzymes with different specificities

e)

coenzyme Systems

86.

The biologically active form of vitamin D is:

a)

7-dehydrocholesterol

b)

ergosterol

c)

1,25-(OH)2 D3

d)

phytosterol

e)

cholesterol

87.

Enzymes are used:

a)

to assess treatment effectiveness

b)

for diagnosis

c)

for treatment

d)

in differential diagnosis

e)

all of the above are correct

88.

Thiamine pyrophosphate is involved in:

a)

amino acid transamination

b)

oxidative decarboxylation of α-keto acids

c)

synthetase reactions

d)

isomerase reactions

e)

hydrolysis reactions

89.

The coenzyme NAD is involved in:

a)

amino acid decarboxylation

b)

one-carbon transfer

c)

redox reactions

d)

biosynthetic reactions

e)

hydrolytic reactions

90.

Cobamide coenzymes contain vitamin:

a)

B2

b)

C

c)

B12

d)

H

e)

A

91.

Ascorbic acid is involved in:

a)

collagen hydroxylation and maturation reactions

b)

redox reactions

c)

free radical scavenging

d)

all of the above are correct

e)

steroid hormone synthesis

92.

Which vitamin affects capillary permeability:

a)

pyridoxine

b)

vitamin P (rutin)

c)

vitamin D

d)

vitamin B1

e)

vitamin B12

93.

Which vitamin is a component of the coenzyme NAD:

a)

E

b)

PP

c)

folic acid

d)

B12

e)

vitamin A

94.

Indicate the difference between enzymes and non-protein catalysts:

a)

catalyze the forward and reverse reactions

b)

reduce the activation energy

c)

have high specificity

d)

exit the reaction unchanged

e)

act at high temperatures

95.

Antirachitic properties are possessed by:

a)

biotin

b)

vitamin C

c)

vitamin D

d)

folic acid

e)

vitamin B1

96.

The optimum pH for the action of most enzymes is:

a)

3.0

b)

9.4

c)

1.5

d)

7.0

e)

5.0

97.

Blood and urine amylase activity is determined to diagnose diseases of:

a)

liver

b)

pancreas

c)

mammary gland

d)

lungs

e)

kidneys

98.

Enzyme inhibitors are substances:

a)

increasing enzyme activity

b)

promoting enzyme cooperation

c)

decreasing enzyme activity

d)

all of the above are correct

e)

are substrates

99.

High ion concentrations Heavy metals:

a)

increase enzyme activity

b)

denature enzyme proteins

c)

stabilize the active site

d)

bind the apoenzyme and coenzyme

e)

activate enzymes

100.

Structures involved in the formation of the active site:

a)

primary

b)

secondary

c)

tertiary

d)

all of the above are correct

e)

supramolecular

101.

Antihemorrhagic properties are possessed by:

a)

biotin

b)

vitamin K

c)

cobalamin

d)

vitamin E

e)

vitamin C

102.

Increasing enzyme concentration with excess substrate:

a)

decreases reaction rate

b)

increases reaction rate

c)

increases the energy barrier

d)

shifts reaction equilibrium

e)

inhibits the enzyme

103.

Enzymes of the hydrolase class catalyze reactions:

a)

oxidation-reduction

b)

biosynthesis of molecules

c)

cleavage of bonds involving water

d)

cleavage of water molecules

e)

isomerization

104.

LDH isoenzyme activity increases in the blood in:

a)

myocardial infarction

b)

protein starvation

c)

hepatitis

d)

acute pancreatitis

e)

diabetes mellitus

105.

General properties of enzymes:

a)

thermolability

b)

specificity

c)

high catalytic activity

d)

presence of a pH optimum

e)

all of the above are correct

106.

Isoenzymes are:

a)

enzymes that catalyze a single reaction

b)

enzymes that use a common catalytic mechanism

c)

multiple forms of a single enzyme

d)

enzymes that have a single coenzyme

e)

all of the above are correct

107.

Responsible for non-hydrolytic cleavage of covalent bonds:

a)

synthetases

b)

isomerases

c)

lyases

d)

transferases

e)

oxidoreductases

108.

Biotin is a coenzyme:

a)

lyases

b)

synthetases

c)

isomerases

d)

oxidoreductases

e)

transferases

109.

Oxidoreductases Coenzymes include:

a)

FAFS

b)

heme

c)

ATP

d)

cobalamin

e)

coenzyme A

110.

Vitamins perform the following functions:

a)

coenzyme

b)

plastic

c)

regulatory

d)

transport

e)

energy

111.

Which vitamin is synthesized by intestinal microflora:

a)

A

b)

D

c)

E

d)

K

e)

B1

112.

The coenzyme FAD contains the vitamin:

a)

B6

b)

B5

c)

B2

d)

E

e)

B1

113.

Castle's intrinsic factor promotes the absorption of vitamin:

a)

C

b)

folic acid

c)

K

d)

B12

e)

B6

114.

The vitamin involved in the hydroxylation of procollagen is:

a)

PP (B3)

b)

biotin

c)

C

d)

B2

e)

A

115.

Absolute specificity of enzymes is characterized by:

a)

conversion of a group of structurally similar substrates

b)

catalysis of substrates with the same bond type

c)

conversion of substrates isolated from a single tissue

d)

catalytic conversion of a single substrate

e)

conversion of different substrates

116.

The main metabolic pathways:

a)

occur in all major tissues of the body

b)

serve to obtain the bulk of energy

c)

are used to synthesize essential macromolecules

d)

answers a b c

e)

are activated only in pathology

117.

Secondary metabolic pathways are characterized by:

a)

appear in pathology

b)

are universal

c)

occur in all cells of the body

d)

are the main suppliers of energy

e)

occur constantly

118.

Accessory metabolic pathways are:

a)

the pentose cycle of glucose metabolism

b)

synthesis of thyroxine from tyrosine

c)

synthesis of adrenaline from tyrosine

d)

answers a b c

e)

the Krebs cycle

119.

Standardization of nutrients includes itself:

a)

conversion of polymers into monomers and energy extraction from them

b)

polymer biosynthesis

c)

substrate reduction processes

d)

all of the above are true

e)

excretion of metabolic products

120.

The pentose cycle is:

a)

a major metabolic pathway

b)

an accessory pathway

c)

a secondary pathway

d)

all of the above are true

e)

an exclusively energy pathway

121.

The anabolic functions of the Krebs cycle are determined by:

a)

the use of the cycle's metabolites for amino acid synthesis

b)

the formation of hydrogen donors for the respiratory chain

c)

the synthesis of pentoses

d)

all of the above are correct

e)

the breakdown of glucose to CO2

122.

The reactions of the Krebs cycle produce:

a)

superoxide anion

b)

ammonia

c)

GTP

d)

NADPH2

e)

hydrogen peroxide

123.

The following vitamins participate in the Krebs cycle:

a)

thiamine

b)

pantothenic acid

c)

PP

d)

riboflavin

e)

all of the above are correct

124.

The functions of the Krebs cycle:

a)

energetic

b)

plastic

c)

integrating

d)

all of the above are correct

e)

hydrogen donor

125.

The Krebs cycle depends on the concentration in the mitochondria of:

a)

oxygen

b)

acetyl-CoA

c)

oxaloacetic acid

d)

NAD/NADH ratio

e)

d) all of the above are correct

126.

The enzymes of the Krebs cycle are localized:

a)

in the mitochondrial matrix

b)

on the outer membrane of the mitochondria

c)

in the nucleus

d)

in the cytoplasm

e)

in lysosomes

127.

The key enzyme of the Krebs cycle is:

a)

citrate synthase

b)

glutathione peroxidase

c)

succinate dehydrogenase

d)

malate dehydrogenase

e)

pyruvate kinase

128.

The Krebs cycle can occur:

a)

only under aerobic conditions

b)

only under anaerobic conditions

c)

at high osmotic pressure

d)

all of the above are correct

e)

only in the cytoplasm

129.

Heme is a coenzyme of:

a)

hydrolases

b)

ATP synthetases

c)

Pepsin

d)

Superoxide dismutase

e)

Cytochromes

130.

The respiratory chain can function:

a)

Only under aerobic conditions

b)

Only under anaerobic conditions

c)

In both of these cases

131.

The enzymes of the respiratory chain are localized:

a)

On the outer mitochondrial membrane

b)

On the inner mitochondrial membrane

c)

In the intermembrane space

d)

In the mitochondrial matrix

e)

In the cytoplasm

132.

The enzymes in the respiratory chain are located:

a)

Depending on the redox potential

b)

Depending on the molecular weight of the protein

c)

Regardless of their redox potential

d)

Depending on the shape of the protein molecule

e)

Randomly

133.

The level of substrate entry into the respiratory chain depends on:

a)

Its molecular weight

b)

Redox potential

c)

The amount oxygen atoms in its structure

d)

The number of carbon atoms in its structure

e)

Water solubility

134.

The functioning of the respiratory chain depends on:

a)

Oxygen entering the cell

b)

Substrates for biological oxidation

c)

The presence of mitochondria

d)

All of the above are correct

e)

The presence of a proton gradient across the inner mitochondrial membrane (or membrane integrity)

135.

The oxidoreductase coenzymes are:

a)

NAD

b)

FAD

c)

FMN

d)

Lipoic acid

e)

All of the above are correct

136.

All substances can be used as substrates in the respiratory chain except:

a)

Isocitrate

b)

Fumaric acid

c)

α-ketoglutarate

d)

Ascorbic acid

e)

Succinic acid

137.

The respiratory chain produces:

a)

Water

b)

Carbon dioxide

c)

GTP

d)

Cyanide

e)

Hydrochloric acid

138.

The mitochondrial respiratory chain includes:

a)

Ubiquinone

b)

FMN

c)

Cytochrome oxidase

d)

FAD

e)

All of the above are correct

139.

The main source of ATP in the body is:

a)

Substrate phosphorylation

b)

Oxidative phosphorylation

c)

Microsomal oxidation

140.

Uncouplers promote the release of energy in the form of:

a)

Heat

b)

ATP

c)

GTP

d)

All of the above are correct

e)

Creatine phosphate

141.

The final metabolite of the respiratory chain is:

a)

Carbon dioxide

b)

Water

c)

Ammonia

d)

AMP

e)

Lactate

142.

Oxidative phosphorylation can occur:

a)

Under aerobic conditions

b)

Under anaerobic conditions

c)

In the cytoplasm

d)

All of the above are correct

e)

In the nucleus

143.

The majority of ATP in the body is formed as a result of:

a)

Glycolysis

b)

Oxidative phosphorylation

c)

Microsomal oxidation

d)

Substrate phosphorylation

e)

Pentose phosphate pathway

144.

Uncouplers of tissue respiration and oxidative phosphorylation can (select two answers):

a)

Inhibit reactions of the Krebs cycle

b)

Block enzyme complexes

c)

Inhibit ATP synthase

d)

Block microsomal oxidation

e)

Activate glycolysis

145.

Uncouplers of tissue respiration and oxidative phosphorylation include:

a)

Amino acids

b)

Glucose

c)

Thyroxine

d)

Adrenaline

e)

Succinate

146.

Barbiturates block:

a)

The Krebs cycle

b)

The transfer of e− and H+ from the cytoplasm to the mitochondria

c)

The transfer of e− and H+ from NADH2 to ubiquinone

d)

Cytochrome oxidase

e)

ATP synthase

147.

Microsomal oxidation is necessary for:

a)

The biosynthesis of some biologically active substances and the detoxification of toxins

b)

ATP formation

c)

The breakdown of polymers in the gastrointestinal tract

d)

Isomerase reactions

e)

Protein synthesis

148.

The main product of the reaction catalyzed by superoxide dismutase is:

a)

Superoxide anion

b)

Hydrogen peroxide

c)

Hydroxyl radical

d)

Water

e)

Oxygen

149.

Hydrogen peroxide is a substrate for:

a)

Catalase

b)

Peroxidase

c)

Glutathione peroxidase

d)

Answers a, b, c

e)

Dehydrogenase

150.

The substrate of catalase is:

a)

Superoxide anion

b)

Hydrogen peroxide

c)

Hydroxyl radical

d)

Water

e)

Oxygen

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