Different functional groups may be found in the structure of L-amino acid residues of proteins. Identify the group that
is able to form ester bond:
A. –SH
B. –NH[sub]2[/sub]
*C. –OH
D. –CH[sub]3[/sub]
E. –CONH[sub]2[/sub]
The structural proteins are involved in maintaining the shape of a cell or in the formation of matrices in the body. Point
out shape of these proteins:
A. Globular
B. Stretch of beads
C. All the proposed
*D. Fibrous
E. Planar
All proteins are divided into simple and conjugated ones. Find out the simple proteins among these ones:
A. Histone
*B. All the proteins presented
C. Albumin of egg
D. Protamine
E. Globulin of egg
There are many important protein functions in the human organism. Point out that of them, which isn't peculiar for
proteins – to be :
A. Antibody
B. Transfer of substances
C. Catalyst
*D. Solvent
E. Structural component of a cell
Histones are related to basic proteins. That is because there is high content of basic amino acid residues in their
structure. Point out these amino acids:
A. Asparagine, Glutamine
*B. Arginine, Lysine
C. Аlanine, Glycine
D. Leucine, Valine
E. Tryptophan, Tyrosine
Biuret test is mainly done for:
A. Dipeptides
*B. Proteins
C. Any of the proposed
D. Polysaccharides
E. Lipids
The isoelectric point (I.P.) of a protein depends upon the amino acids composition of the protein. Choose the amino
acid which high content in protein molecule decreases its I.P. value:
*A. Aspartic acid
B. Аlanine
C. Leucine
D. Histidine
E. Tryptophan
Primary structure of proteins is formed due to one type of bonds. Point out it:
A. Hydrogen bond
B. Metal bond
*C. Peptide bond
D. Ester bond
E. Disulfide bond
Protein properties may be changed under the influence of some factors. Find out them:
A. The temperature of the environment
*B. All the factors that are present
C. Strong alkaline medium
D. Strong acidic medium
E. Organic solvent
All are aromatic amino acids EXCEPT:
A. Tyrosine
B. Phenylalanine
C. All the positions are correct
*D. Lysine
E. Tryptophan
The mixture of proteins can be separated by salting-out. Specify the reagent formula that is used for this purpose:
A. HNO[sub]3[/sub]
B. H[sub]3[/sub]PO[sub]4[/sub]
C. C[sub]2[/sub]H[sub]5[/sub]OH
*D. NaCl
E. C[sub]6[/sub]H[sub]6[/sub]
The yellow color sediment appearance after the addition of strong nitric acid to albumin solution is due to the
presence of aromatic acid residues in protein composition. Choose those one:
*A. L-tyrosine
B. L-alanine
C. L-serine
D. L-proline
E. L-methionine
Alpha- helix and Beta -pleated sheet are examples of:
*A. Secondary structure
B. Tertiary structure
C. Quaternary structure
D. All positions are wrong
E. Primary structure
Polypeptide chains of collagen include specific amino acids. Name one of them:
A. Formyl-methyonine
B. Cysteine
C. Beta-alanine
*D. Hydroxyproline
E. Ornithine
What class of proteins Albumins and Globulins are related to?
A. Lipoproteins
B. Metalloproteins
C. Glycoproteins
*D. Simple proteins
E. Chromoproteins
What type of amino acids mainly is represented as residues in proteins of human body?
A. D-beta-amino acids
B. D-alpha-amino acids
*C. L-alpha-amino acids
D. L-beta-amino acids
E. D-alpha-imino acids
The proteins are able to carry out the regulatory function. Find out those protein:
A. Aminopeptidase
B. Collagen
C. Hemoglobin
*D. Insulin
E. Immunoglobulin G
The polypeptide chain gets the globular structure after the formation of various bonds between the radicals of amino
acid residues. Specify the strongest bond in the globular structure:
A. Hydrogen bond
*B. Disulfide bond
C. Electrostatic interaction
D. Hydrophobic interaction
E. Donor-acceptor bond
F. Sodium hydroxide
What physical-chemical property is observed for fibrous protein only?
A. Denaturation and renaturation
B. Solubility in water
C. Amphoteric properties
*D. Elasticity
E. Solubility in lipids
Half saturation test using salting-out is done for:
A. Fibrin
*B. Globulin
C. Albumin
D. Prothrombin
E. Haemoglobin
Ninhydrin is a reagent to prove the presence of alpha-amino group in the structure of amino acid due to change of its
color (violet color is observed). Choose the amino acid whose solution changes the color of this reagent in other way
– it becomes yellow:
A. L-tyrosine
B. L-alanine
C. L-serine
*D. L-proline
E. L-methionine
The content of these amino acids in the composition of acidic protein Pepsin is too big in comparison with the content
of other amino acids in it. Name them:
A. Valine and Leucine
*B. Aspartic acid and Glutamic acid
C. Lysine and Arginine
D. Alanine and Glycine
E. Tyrosine and Tryptophan
Protonation and deprotonation at neutral pH occurs for one amino acid from following list. Point out it:
A. Tryptophan
*B. Histidine
C. Glycine
D. Aspartic acid
E. Alanine
Which of the following bonds are intact during denaturation of proteins:
A. Hydrogen bonds
B. All positions are correct
C. Ionic bonds
D. Hydrophobic bonds
*E. Peptide bonds
The solubility of proteins in saline solutions is determined by their native structure. Point out the protein, which will
swell only in saline solution:
A. Albumin
B. Myoglobin
C. Pepsin
D. Immunoglobulin
*E. Elastin
The isoelectric point of simple protein equals 7.2. Propose the pH of buffer solution used for the electrophoresis
method to separate this protein from the mixture with a condition to leave it on the start line of carrier:
A. pH=5.0
*B. pH=7.2
C. pH=7.4
D. pH=7.0
E. pH=7.6
How many polypeptide chains (the least number) may be represented in quaternary structure of protein molecule?
A. Five
*B. Two
C. Four
D. One
E. Three
Point out the type of bond allowing the formation of alpha-helix structure:
*A. Hydrogen bonds between peptide fragments
B. Hydrogen bonds between side-chain radicals
C. Electrostatic interaction
D. Ester bond between side chain radicals
E. Disulfide bond between two cysteine radicals
Proteins are obligatory components of human diet. Specify the function of proteins in this case:
*A. Nutritive
B. Catalytic
C. Structural
D. Transport
E. Regulatory
Choose the factor that causes the sedimentation of protein in solution without denaturation:
A. Nitric acid
*B. Ammonia sulfate
C. Toluene
D. Sulfuric acid
E. Sodium hydroxide
What amino acid high content presence in the composition of polypeptide chain does not allow the formation of
alpha-helical structure as secondary level of organization?
A. Alanine
B. Threonine
C. Glycine
D. Serine
*E. Proline
The tertiary structure of protein is formed mainly due to disulfide bonds between side radicals of one amino acid, only.
Point out it:
A. Lys
B. Asp
C. His
*D. Cys
E. Met
The molecule of simple protein insulin contains two polypeptide chains. Specify the level of protein organization, at
which the insulin is able to act as hormone:
A. Primary
B. Secondary
*C. Quaternary
D. Tertiary
E. A conformation after limited proteolysis
Toxic affection of liver results in dysfunction of protein synthesis. It is usually accompanied by the following kind of
dysproteinemia:
*A. Absolute hypoproteinemia
B. Paraproteinemia
C. Relative hypoproteinemia
D. Absolute hyperproteinemia
E. Relative hyperproteinemia
Choose, please, the blood serum index used for estimation of hyperproteinemia state:
*A. The total content of proteins
B. The amino acid concentration
C. The content of acute phase proteins
D. The total activity of all the enzymes
E. The content of albumins
The conjugated protein necessarily contains special component as a non-protein part. Choose the substance that
can't carry out this function:
A. Phosphate anion
B. Monosaccharide
*C. HNO₃
D. Heme
E. Fe[sup]2+</sup>
What compound serves as non-protein part of glycoproteins:
A. Heme
B. Copper ion
C. Phospholipid
D. Ferric ion
*E. Galactose
Point out a possible cause of hyperproteinemia
A. Nephritic syndrome
B. Diabetes mellitus
C. Affected gastrointestinal tract
*D. Infection (disturbed the macrophage system)
E. Increased permeability of the capillary wall
The hormone receptors are related to the class of conjugated proteins. Name it:
A. Lipoproteins
B. Nucleoproteins
C. Flavoproteins
D. Chromoproteins
*E. Glycoproteins
Triacylglycerols (TG) are synthesized in the liver but are stored in adipose tissue. Name the class of proteins
promoted the transport of TG from the liver to adipocytes:
A. Phosphoproteins
B. Metalloproteins
C. Glycoproteins
D. Chromoproteins
*E. Lipoproteins
The diseased person with diagnosis acute kidney insufficiency is in urological department of hospital. Choose the
method for cleaning of this person`s blood from low-molecular compounds which can cause toxic effect in the
organism:
A. Electrophoresis
B. Affine chromotography
C. Hydrolysis
D. Salting-out
*E. Dialysis
The conjugated protein necessarily contains special component as a non-protein part. Choose the substance that
can't carry out this function:
*A. Salt of Hg[sup]2+</sup>
B. Glucose
C. AMP
D. Thiamine pyrophosphate
E. ATP
Albumins of blood plasma are negative charged under the condition of electrophoresis method duration. What
electrode type will you choose for albumins directed movement in the electric field?
A. Silk electrode
B. Catode
C. Carbon electrode
D. Calomel electrode
*E. Anode
Ceruloplasmin (the protein of blood plasma) contains copper ion and therefore has blue color. Name the class of this
protein:
A. Nucleoprotein
*B. Chromoproteins
C. Phosphoproteins
D. Lipoproteins
E. Glycoproteins
The electrophoresis method is used for the separation of blood plasma proteins. Name the parameter of the protein
molecule that is in need to determine the pH of buffer solution for separation of proteins in electrophoresis method:
A. The solubility in lipids
B. The diameter of the molecule
C. The mass of the molecule
*D. Isoelectric point
E. The solubility in the water
Which method is better suited to separate a mixture of compounds into its individual components and detects small
amounts (microgram or even picogram) of material:
A. Spectrophotometry
B. Dialysis
C. Salting out
*D. Paper chromatography
E. Ultracentrifugation
Point out a possible cause of hypoproteinemia:
*A. Affected liver cells
B. Paraproteinemia
C. Decreased permeability of the capillary wall
D. Overeating
E. Multiple myeloma
The enzyme preparation cytochrome C is used for the improvement of tissue respiration in newborns at asphyxia
state. Name the class of this conjugated protein:
A. Nucleoproteins
*B. Chromoproteins
C. Glycoproteins
D. Flavoproteins
E. Lipoproteins
It is in need to use the heme with iron ion for the active centers of cytochrome C oxidase (the key enzyme of tissue
respiration). Name the class of this conjugated protein:
A. Flavoproteins
B. Lipoproteins
C. Nucleoproteins
*D. Chromoproteins
E. Glycoproteins
Which method is appropriate for the determination of total protein content in the blood serum:
A. Dialysis
B. Electrophoresis
*C. Biuretic method
D. Fole’s test
E. Salting out
Name the class of proteins used for the formation of ribosome subunits:
A. Flavoproteins
B. Lipoproteins
C. Glycoproteins
D. Phosphoproteins
*E. Ribonucleoproteins
Which group of proteins being phosphoproteins posses an activity but being dephosphorylated has lost the activity:
A. Transfer of vitamins
B. Hormones
C. Transfer of lipids
D. Carriers through membrane
*E. Enzymes
Choose the conjugated protein in possession of following characteristics: quaternary structure - 4 polypeptide chains;
non-protein part – 4 hemes; function – oxygen transport in the blood:
A. Ceruloplasmin
*B. Hemoglobin
C. Low Density Lipoprotein
D. Albumin
E. Immunoglobulin
All the proteins are divided into simple and conjugated ones. Find out the conjugated protein among these ones:
A. Egg albumin
B. Protamine
C. Egg globulin
D. Histone
*E. Myoglobin
There is the use of electrophoresis for separation of proteins of blood plasma to prove diagnosis of diseased persons.
Name the property of proteins that is the basis for the principle of electrophoresis method:
A. The big mass of the molecule
B. The ability of swelling
*C. The net charge of the molecule
D. Optical activity
E. The high viscosity of the solution
The phosphorylation (the attraction of phosphate group to the substrate) of polypeptide chain is often used for
stimulation of biological activity of a protein. Name the class of conjugated protein formed due to phosphorylation:
A. Glycoproteins
B. Chromoproteins
C. Nucleoproteins
*D. Phosphoproteins
E. Lipoproteins
Ultracentrifugation is in need in biochemical investigations for:
A. The separation of low-molecular compounds
B. The investigation of chemical composition of organic compound
C. The determination of primary structure of proteins
D. The study of three-dimensional structure of the molecule
*E. The receiving of subcellular fractions of a cell
Flavoproteins are usually catalysts in a cell due to the presence of special vitamin fragment in their structure. Name
this vitamin:
A. Folic acid
B. Ascorbic acid
*C. Riboflavin
D. Nicotin amide
E. Pantothenic acid
Proteoglycans are conjugated proteins containing different polypeptide chains of core protein and glucose
aminoglycan moiety. Choose the class of conjugated protein that is related to proteoglycan:
A. Nucleoprotein
B. Chromoprotein
*C. Glycoprotein
D. Lipoprotein
E. Phosphoprotein
Complex proteins do various functions. Find out the function of hemoglobin in erythrocytes:
A. Catalytic function
*B. Transport function
C. Nutrition function
D. Regulatory function
E. Protection against viruses
Name the location of deoxyribonucleoproteins in eukaryotic cell, but not in the nucleus:
A. Cytoplasma
B. Microsome
C. Lisosome
D. Endoplasmic reticulum
*E. Mitochondria
“All biological catalysts are not proteins” This statement is justified by this notion:
*A. RNAs can act as ribozymes
B. All enzymes do not follow the Michaelis-Menten hypothesis
C. Enzyme activity may be controlled by hormones
D. Metal ions are involved in attachment to enzymes
E. Antibodies take part in the catalysis of many reactions
Some terms are used for the description of non-protein part of an enzyme. Point out the term for non-protein part that
easily dissociates from polypeptide chain:
A. Metal ions
*B. Coenzyme
C. Prosthetic group
D. Cofactor
E. Apoenzyme
In case of enterobiasis acrihine - the structural analogue of vitamin B<sub>2</sub> - is administered. The synthesis
disorder of which enzymes does this medicine cause in microorganisms?
*A. FAD-dependent dehydrogenases
B. Peptidases
C. Cytochromeoxidases
D. NAD-dependet dehydrogenases
E. Aminotransferases
There are different cofactors in the structure of conjugated enzymes but only one is used for transfer of amine group
from amino acid to keto acid. Name it:
A. Carboxybiotin
B. FAD
C. NAD<sup>+</sup>
D. Thiamine pyrophosphate
*E. Pyridoxal phosphate
The enzyme hexokinase can catalyze the conversion of glucose or fructose in tissues. Find out the type of this
enzyme specificity:
A. Stereochemical
*B. Relative group
C. Absolute relative
D. Absolute group
E. Absolute
The change of the temperature of environment from 0<sup>o</sup>C to 38<sup>o</sup>C can cause this effect on
enzyme molecule:
A.
B. The substrate molecular charge changes
C. The enzyme molecular charge changes
D. Enzyme action specificity varies
E. A denaturation of enzymes occurs
*F. The probability of enzyme-substrate complex formation is increased
Name the vitamins whose derivatives are used for the formation of oxidoreductase structure:
A. H, D
B. C, P
*C. B<sub>2</sub>, B<sub>3</sub>
D. A, E
E. B<sub>6</sub>, B<sub>9</sub>
The pancreatic amylase is in need to cleave the alpha-1.4-glycosidic bonds in the structure of polysaccharides using
the water as the substrate. Specify the class of this enzyme:
A. Isomerase
*B. Hydrolase
C. Ligase
D. Lyase
E. Oxido reductase
Some terms are used for the description enzyme components. Point out the term of a protein part of conjugated
enzyme:
*A. Apoenzyme
B. Metal ions
C. Coenzyme
D. Prosthetic group
E. Cofactor
Point out the factor that can cause the damage of enzyme function in a cell:
*A. The surplus of protons in a cell
B. The presence of a product of enzymatic reaction
C. pH medium about 7.2
D. Temperature 37<sup>o</sup>C
E. The presence of activator of enzyme
The oxidation of a substrate may be catalyzed by enzyme - flavoprotein that contains FAD as prosthetic group.
Name, please, the vitamin used for this non-protein part of enzyme formation:
A. Biotin
B. Nicotinamide
*C. Riboflavin
D. Ascorbic acid
E. Adenosine triphosphate
LDH1 and LDH2 levels are raised in the following organ damage:
*A. Heart, RBC
B. Brain, heart, liver
C. Heart, kidney, liver
D. Liver, brain, kidney
E. Brain, bones, liver
Chymotrypsin is the proteolytic enzyme catalyzing the cleavage of peptide bonds in any protein molecule. Name the
class of this enzyme:
A. Ligase
*B. Hydrolase
C. Lyase
D. Isomerase
E. Oxidoreductase
Enzymes mediating transfer of a structural fragment from one molecule to another are:
A. Peptidases
B. Oxidases
C. Ligases
D. Lyases
*E. Transferases
One of the important properties of enzymes is their specificity of action. Check up a type of specificity for salivary
amylase:
A. Absolute
B. Absolute relative
C. Absolute group
*D. Relative group
E. Stereochemical
Which bond is cleaved by Alpha amylase in oral cavity?
A. Beta 1-4 glycosidic
B. Beta 1-6 glycosidic
C. Ester bond in any ester structure
*D. Alpha 1-4 glycosidic
E. Alpha 1-6 glycosidic
In clinical practice tuberculosis is treated with izoniazid preparation – that is an anti-vitamin able to penetrate into the
tuberculosis bacillus. Tuberculostatic effect is induced by the interference with replication processes and oxidationreduction reactions due to the buildup of pseudo-coenzyme:
A. CoQ
B. TDP
C. FAD
D. FMN
*E. NAD
ATP molecules may be used for Transferases and Ligases function. Point out the signs of ATP use for Ligases class:
A. ATP is used for a substrate decarboxylation.
B. ATP is used for hydrolysis of a substrate bond
C. ATP is used for a substrate phosphorylation
*D. ATP is used for the new bond formation during the interaction of two substrates
E. ATP is used for a substrate dephosphorylation
The active centre of simple enzyme is composed from:
A. The cofactor and prosthetic group
*B. Some amino acid residues of polypeptide chain placed in the same spatial fragment
C. The terminal amino acid residues
D. Linear fragment of polypeptide chain
E. One polypeptide chain completely
There are some characteristic sites in the enzyme structure. Choose the most important site for enzyme function:
A. A site containing Asp and Glu
B. Apoenzyme
C. Cofactor
D. Allosteric centre
*E. Active centre
The catalytic site of active center of enzyme is used for:
A. Binding with inhibitor
B. Binding with the substrate
C. Binding with activator
*D. Conversion of a substrate in the reaction
E. Removal of a product of the reaction
Researchers isolated five isozymes of Lactate dehydrogenase from human blood serum and studied their properties.
What property of these isozymes indicates that they are genetic forms of the same enzyme?
A. The same net charge of the molecule
*B. They catalyze the same reaction
C. They have the same molecular weight
D. The same electrophoretic mobility
E. The same tissue localization
A qualitative composition of product molecule is completely identical to substrate one, but the structure is different.
Name the enzyme class:
A. Oxidoreductase
B. Lyase
C. Ligase
*D. Isomerase
E. Hydrolase
Coenzyme forms are correctly matched to vitamins except one. Point out it:
A. Biotin – carboxylated biotin
*B. Vitamin B<sub>1</sub> - ATP
C. Pantothenic acid – CoASH
D. Niacin – NAD<sup>+</sup> + NADP<sup>+</sup>
E. Vitamin B2 – FMN + FAD
Enzymes are the catalysts of protein nature. Name the property of enzymes which is not represented at the inorganic
catalysts:
A. Big half-life
B. Inert to chemical substrates
C. Wide specificity
D. Ability to lowering the energy to activate the reaction
*E. Ability to the denaturation
Conjugated enzymes contain cofactors in their structure. Point out the location of vitamin derivative cofactor in the
structure of enzyme:
A. Hydrophobic fragment of structure
B. Near the metal-ion-cofactor in the structure
C. Hydrophilic fragment of structure
*D. Active centre
E. Allosteric centre
Which of the following is the reaction that is catalyzed by lyase:
A. Oxidative decarboxylation
*B. Dehydration
C. Hydrolysis
D. Acetylation
E. Oxidation
Name, please, the principle base used for the classification of enzymes:
A. Chemical structure of products for enzymatic reaction
B. Type of energy conversion
C. Chemical structure of enzyme
*D. Type of chemical reaction catalyzed by enzyme
E. Chemical structure of non-protein part of the enzyme
The relative group specificity may be found for enzymes catalyzing the digestion of proteins in the gastrointestinal
tract. Find out their trivial name:
A. Urease
B. Protein phosphatase
C. Protein kinase
*D. Peptidase
E. Transaminase
Only one factor can influence on the charge of amino acid radicals in the enzyme active centre. Name it:
A. Pressure
B. Temperature
C. The surplus of a reaction product
*D. pH medium
E. The presence of a competitive inhibitor
There are some factors influencing human enzyme activity. Point out one of them resulting in complete loss of
enzymatic activity:
A. Сarbon dioxide
B. Sodium chloride solution
C. Vitamin H
*D. T = 100<sup>o</sup> C
E. P =101325 Pa
Oxidoreductase can contain prosthetic group with vitamin B<sub>2</sub>. Name it:
*A. Flavin adenine dinucleotide (FAD)
B. Pyridoxal phosphate
C. Retinal
D. Ascorbic acid
E. Nicotinamide adenine dinucleotide (NAD<sup>+</sup>)
Sulfonamides are used as drugs to protect our organism from some foreign bacteria. Enzyme in bacterial cell
producing folic acid from para-aminobenzoate is inhibited by this group of drugs. Choose the type of inhibition for
sulfonamides:
*A. Competitive
B. Allosteric
C. Suicide
D. Uncompetitive
E. Noncompetitive
The common enzymatic reaction may be represented so: E + S <-> ES <-> ES <-> EP <-> E + P. Try to name using
this equation all the factors that can influence the rate of this reaction:
*A. The concentration of a substrate, enzyme, product and stability of ES-complex
B. The concentration of a substrate, only
C. The concentration of enzyme-substrate complex, only
D. The concentration of enzyme, only
E. The concentration of a substrate, enzyme and product, only
Cholesterol synthesis is regulated by feed-back mechanism. Name the allosteric inhibitor of key enzyme for this
synthesis:
*A. Cholesterol
B. ATP
C. ADP
D. Glucose
E. NADPH
Choose the factor that changes the cytoplasmic enzyme conformation mainly:
A. Suicide inhibitor
*B. Allosteric inhibitor
C. Water
D. Environmental temperature value about 25<sup>o</sup> C
E. Environmental pH value about 7.4
A majority of key enzymes contain the allosteric centre. Specify a role of this centre:
A. It changes the structure of the substrate
*B. It attaches the regulatory factor
C. It blocks the active centre
D. It promotes the dissociation of a coenzyme
E. It attaches the substrate
Salivary amylase activity may be decreased by:
A. The increase of temperature from 38<sup>o</sup>C to 65<sup>o</sup>C
B. The decrease of temperature from 38<sup>o</sup> C to 25<sup>o</sup>C
*C. All the changes described may be in need
D. The change of pH from 6,8 to the value 5,5
E. The addition of copper sulfate
Suicide type of inhibition is considered when:
*A. There is the intermediate metabolite formation from the inhibitor which tightly binds to the active centre of enzyme
to block it
B. The product of reaction is the allosteric inhibitor for enzyme
C. The inhibitor structure is similar to substrate one
D. The end-product of reaction is not removed from the environment
E. The end-product of reaction binds to the structure of the substrate to give non-soluble complex
Point out the type of bonds that are formed between Ser, Tyr and Cys residues in active centre of the enzyme and
the molecule of substrate containing functional group: --COOH:
A. Disulfide and ester bonds
B. Hydrophobic interactions, only
C. Ester bond and hydrophobic interaction
*D. Ester and hydrogen bonds
E. Disulfide bond and hydrophobic interaction
Glycogen phosphorylase b is transformed to the active form a by the action of special kinase with the use of ATP as
donor of phosphate group. Find out, please, the type of enzyme activation:
A. Limited proteolysis
B. Activation by Ca<sup>2+</sup>
C. The change of pH medium
*D. Covalent modification
E. Competitive inhibition
Heme synthesis starts from glycine and succinyl-SCoA interaction with delta-aminolevulinate synthetase help. It is
inhibited by the terminal metabolic product - heme. Name the inhibition type:
A. Competitive Inhibition
B. Uncompetitive Inhibition
C. Limited proteolysis
*D. Feedback Inhibition
E. Non-competitive Inhibition
Covalent modification of inactive form of enzyme may be catalyzed by special enzyme in a cell. Name it:
A. Hydroxylase
*B. Protein kinase
C. Oxygenase
D. Esterase
E. Ligase
Succinate dehydrogenase catalyses the dehydrogenation of succinate. Malonic acid HOOC-CH2-COOH is used to
interrupt the action of this enzyme. Choose the inhibition type:
A. Allosteric
B. Limited proteolysis
*C. Competitive
D. Non-competitive
E. Dephosphorylation
Point out the probable way of proenzyme transformation to the active enzyme:
A. Inhibitor action
B. Vitamin non-protein part dissociation from enzyme
*C. Limited proteolysis
D. Decarboxylation
E. Dehydration
E. Fisher`s theory explains the mechanism of enzyme action with the fixed type of specificity, only. Name it:
A. Absolute relative
B. Relative group
C. Stereochemical
D. Absolute group
*E. Absolute
The formation of ES complex is due to various types of bonds between E and S. Specify the type of bond, which is
usually formed between charged functional groups in this case:
A. Hydrophobic interaction
B. Peptide bond
*C. Electrostatic interaction
D. Donor-acceptor bond
E. Hydrogen bond
Name, please, the inhibitor for salivary amylase:
A. Potassium cyanide
B. Alanine
*C. Copper sulfate
D. Hydrogen peroxide
E. Sodium chloride
Point out the activator used for the determination of amylase activity:
A. CuSO₄
*B. NaCl
C. H₃PO₄
D. Ca²⁺
E. ATP
Name, please, the factors that must be in constant levels during the investigation of enzyme concentration influence
the velocity of enzymatic reaction:
A. Substrate concentration
B. The temperature
*C. All the factors proposed must be in constant levels
D. Activator concentration
E. pH of the environment
Choose the name of scientists whose experiments are recognized as the basis in understanding of “induced fit”
theory for mechanism of enzymatic reaction:
A. Fisher E.
*B. Koshland D.
C. Haldane R.
D. Menten M.
E. Michaelis L.
The affinity of enzyme molecule to a substrate may be estimated using the value of:
A. The initial velocity of the reaction
B. V_max for reaction duration
*C. K_m for the enzyme
D. pH of the environment
E. The temperature
Covalent catalysis as mechanism of enzyme catalysis was studied in experimental works with one proteolytic
enzyme. Find out it:
A. Pepsin
B. Aldolase
C. Glucoisomerase
D. Decarboxylase
*E. Chymotrypsin
Competitive inhibitor always interacts with enzyme active centre. Find out the explanation of this phenomenon:
A. Inhibitor is an exact copy of a substrate structure
B. Inhibitor is similar to the product's structure
C. Inhibitor forms a covalent type of bonds with amino acid residues of active centre
*D. Inhibitor is similar to a substrate structure
E. Inhibitor causes the denaturation of active centre
Name, please, the equation for V-[S] dependence for the moment of complete saturation of all the active centers of
enzyme molecules:
A. V= k•V_max
B. V=V_max •[S]/K_m+[S]
C. V=V_max / K_m + [S]
D. V=k• [S]
*E. V=V_max
Find out, please, the factor used to change the charge of functional groups both in the active centre of enzyme and in
the substrate molecule:
A. The addition of activator to the environment
B. All the factors proposed may be in need
C. The temperature of environment
*D. The pH of environment
E. The addition of competitive inhibitor to the environment
The common feature of an enzyme-cascade system regulation is:
*A. Feed back inhibition
B. Competitive inhibition
C. Counter-regulation
D. Amplification
E. Suicide inhibition
The regulation of the enzymatic activity is carried out by different ways. Point out the way that is used more often in
the regulation of key enzymes:
A. The change of pH medium
*B. Allosteric regulation
C. Activation by Ca²⁺
D. Competitive inhibition
E. Limited proteolysis
Choose the method that is more often used for the determination of inhibitor type:
A. Michaelis-Menten graphical method
B. Nuclear magnetic resonance method
C. Eadie-Hofstee graphical method
*D. Lineweaver-Burk graphical method
E. Briggs-Haldane graphical method
Disopropyl phosphofluoride (DFP) reacts with serine proteases irreversibly and therefore is:
A. A stimulator
B. Allosteric inhibitor
C. Non-competitive inhibitor
*D. Affinity label
E. Competitive inhibitor
Find out the parameter that is changed in the incubation phase of experimental test tube for the determination of
choline esterase activity in the blood plasma:
A. The acetic acid content
B. The choline concentration
*C. All the positions are right
D. The acetylcholine concentration
E. The pH
Twelve hours after an accute attack of retrosternal pain a patient presented a jump of aspartate aminotransferase
activity in blood serum. What pathology is this deviation typical for?
A. Viral hepatitis
B. Diabetes insipidus
C. Collagenosis
*D. Myocardium infarction
E. Diabetes mellitus
Find out the activator used for amylase activity determination in the urine of patient:
*A. Starch
B. Ammonia sulfate
C. Sodium chloride
D. Pyruvate
E. Copper sulfate
Point out the signs of multiple enzyme systems (MS):
A. The MS enzymes form several different metabolic products at once
B. The MS enzymes are united by their intracellular localization
C. The MS enzymes form a single structural-functional complex
*D. All that is described is right
LDH1 and LDH2 levels are raised in the following organ damage
A. Heart, kidney, liver
*B. Heart, RBC, kidney
C. Liver, brain, kidney
D. Brain, bones, liver
E. Brain, heart, liver
Find out the pathological state associated with the decrease of choline esterase activity in the blood serum of patient
A. Acute pancreatitis
B. Gout
C. Influenza
D. Myeloma
*E. Viral hepatitis
Marked increase of activity of МВ-forms of CPK (creatine phosphokinase) and LDH-1 were revealed on the
examination of the patient's blood. What is the most likely pathology?
A. Hepatitis
B. Cholecystitis
C. Rheumatism
D. Pancreatitis
*E. Miocardial infarction
Lactate dehydrogenase (LDH) isozymes catalyze the transformation of pyruvate to lactic acid in different types of
tissues. Point out the structural distinctive peculiarity of each LDH isozyme:
A. Different level of structural organization in native molecule
B. Different active center structure
C. Different by the quantity of subunits
*D. Different by the combination of subunits, forming a native molecule
E. Different by the type of coenzyme in native molecule
6 hours after the myocardial infarction a patient was found to have elevated level of lactate dehydrogenase in blood.
What isozyme should be expected in this case?
A. LDH3
B. LDH5
C. LDH2
*D. LDH1
E. LDH4
During metabolic process active forms of the oxygen including superoxide anion radical are formed in the human
body. With help of what enzyme is this anion inactivated?
A. Catalase
B. Peroxidase
C. Glutathione peroxidase
D. Glutathione reductase
*E. Superoxide dismutase
The cytoplasm fraction of tissue homogenate has been obtained for some enzyme activity determination. Point out
the enzyme whose activity may be determined in this fraction:
*A. Glucokinase
B. Trypsin
C. Maltase
D. Urease
E. Pepsin
Pyruvate dehydrogenase complex is multiple enzyme system because it contains:
A. Two enzymes and one coenzyme
B. Two enzymes and five coenzymes
*C. Three enzymes and five coenzymes
D. Five enzymes and five coenzymes
E. Three enzymes and three coenzymes
Profuse foam appeared when dentist put hydrogen peroxide on the mucous of the oral cavity. What enzyme caused
such activity?
*A. Catalase
B. Acetyltransferase
C. Cholinesterase
D. Glucose-6-phosphatdehydrogenase
E. Methemoglobinreductase
Total activity of enzyme depends on the:
A. pH medium
B. Temperature medium
C. Substrate concentration
*D. All the factors described
E. Enzyme concentration
A patient presents high activity of LDH1, LDH2, aspartate aminotransferase, creatine phosphokinase. In what organ
(organs) is the development of a pathological process the most probable?
A. In connective tissue
B. In kidneys and adrenals
*C. In the heart muscle (initial stage of myocardium infarction)
D. In skeletal muscles (dystrophy, atrophy)
E. In liver and kidneys
Patient’s amylase activity in the urine excesses the normal values in ten times as much. Point out the possible
diagnosis:
A. Angina
B. Influenza
C. Viral hepatitis
D. Diabetes mellitus
*E. Sharp pancreatitis
The activity of choline esterase in the blood serum of patient equals 95 micromole/sec• L. Propose, please, the way
for the transformation of this value into units [mmole/L*min]:
A. Divide this result into 1000, only
B. Multiple this result into 60 times, only
C. Divide this result into 60, only
D. Multiple this result into 1000 times, only
*E. Divide this result into 1000 times, and multiple on 60
Find out the parameters that are in need to calculate specific activity of enzyme:
A. The pH value of the environment and turnover number
B. The volume of the test sample and total activity
*C. The protein content in the test sample and total activity
D. Turnover number and total activity
E. The product concentration in the test sample and total activity
The rate limited step for Citric Acid Cycle duration is the reaction catalyzed by:
A. Alpa-ketoglutarate dehydrogenase
B. Citrate synthase
*C. Isocitrate dehydrogenase
D. Cis-Aconitase
E. Malate dehydrogenase
Find out, please, the enzyme whose activity is inhibited mainly under the accumulation of ATP in the matrix of
mitochondria:
A. Malate dehydrogenase
B. Fumarase
*C. Citrate synthase
D. Aconitase
E. Alpha-ketoglutarate dehydrogenase
Isocitrate was used as an oxidized substrate in the experiment with isolated mitochondria. Specify the substance that
can inhibit the isocitrate oxidative decarboxylation:
A. Glucose
B. cAMP
*C. ATP
D. Citrate
E. ADP
Krebs Cycle is an amphiobolic way. Choose the explanation of this sentence:
*A. Metabolites of Krebs Cycle may be used in anabolic pathways
B. The process is in mitochondrion
C. The process forms CO[sub]2[/sub] and H[sub]2[/sub]O
D. The process forms NADH
E. One mole of ATP is formed in one cycle
Magnesium and Manganese ions are in need for the function of one enzyme from this register, only. Point out it:
A. Aconitase
B. Malate dehydrogenase
C. Fumarase
*D. Isocitrate dehydrogenase
E. Succinate dehydrogenase
Name the regulatory enzyme from Citric Acid Cycle whose activity is stimulated by allosteric activator ADP at
condition of its accumulation in the matrix of mitochondria:
A. Citrate synthase
B. Cis-Aconitase
C. Succinate dehydrogenase
D. Alpa-ketoglutarate dehydrogenase
*E. Isocitrate dehydrogenase
Vitamin B[sub]1[/sub] (coenzyme TPP) is necessary for only one dehydrogenase function in Krebs Cycle. Point out it:
A. Malate dehydrogenase
*B. Alpha-Ketoglutarate dehydrogenase
C. Lactate dehydrogenase
D. Isocitrate dehydrogenase
E. Succinate dehydrogenase
Two reactions of Krebs Cycle are named as oxidative decarboxylation. Point out the enzyme for this type of reaction:
A. cis-Aconitate hydratase
B. Succinyl~SCoA synthase
C. Citrate synthase
D. Succinate dehydrogenase
*E. Isocitrate dehydrogenase
Name, please, the process that is related to the second phase of catabolic pathways in humans:
A. Proteolysis
B. Krebs cycle
C. Gluconeogenesis
D. Ammonia utilization in Urea cycle
*E. Glycolysis
Exogenous substances may be involved in catabolic pathways to be used as energy sources for humans EXCEPT:
A. Alcohol
B. Fatty acids
C. Amino acids
*D. Vitamins
E. Monosaccharides
All these metabolic pathways or processes take place inside the mitochondria except:
A. Oxidative phosphorylation
*B. Glycolysis
C. Krebs cycle
D. Urea cycle
E. Fatty acid beta-oxidation
Name, please, the class of organic compound usually used as energy source for anabolic pathways in humans:
A. Carboxylic acids
B. Nucleosides
C. Alcohols
D. Monosaccharides
*E. Nucleoside triphosphates
Fluroacetate inhibits:
A. Alpha-ketoglutarate dehydrogenase
B. Malate dehydrogenase
C. Succinate dehydrogenase
D. Citrate synthetase
*E. Cis-Aconitase
Oxidative decarboxylation reactions occur two times in Citric Acid Cycle, but the mechanism of these reactions is not
the same. Choose the conversion that may be named as oxidative decarboxylation and catalyzed by multienzyme
system:
*A. Alpa-ketoglutarate is converted to Succinyl-CoA
B. Citrate is converted to Cis-Aconitate
C. Isocitrate is converted to Alpa-ketoglutarate
D. Succinate is converted to Fumarate
E. Malate is converted to Oxaloacetate
Name, please, the organic compound formed in Krebs cycle due to substrate phosphorylation:
*A. GTP
B. ATP
C. GDP
D. Isocitrate
E. Citrate
The accumulation of NADH in the matrix of mitochondria is the signal to inhibit:
A. Cis-Aconitase
*B. Isocitrate dehydrogenase
C. Malate dehydrogenase
D. Citrate lyase
E. Fumarase
How many moles of high energy bond containing compound are produced due to substrate phosphorylation in one
round of Citric Acid Cycle:
A. Twelve
B. Two
C. Four
*D. One
E. Three
Nucleoside triphosphate is formed in Krebs Cycle. Point out its abbreviation:
A. ATP
B. CTP
C. UTP
D. TTP
*E. GTP
Krebs cycle is regulated by the ATP/ADP ratio in aerobic cell. Point out the value of this ratio that causes the
stimulation of Krebs Cycle duration:
A. _3
B. _1
C. _5
*D. _0.5
E. _2.5
Only one dehydrogenase of Krebs Cycle has the non-protein part FAD. Name it:
A. Isocitrate dehydrogenase
B. Malate dehydrogenase
C. Pyruvate dehydrogenase
*D. Succinate dehydrogenase
E. Alpha-Ketoglutarate dehydrogenase
Name, please, the initial substrates for Krebs cycle (first reaction):
*A. Acetyl-CoA and oxaloacetate
B. Citric acid, only
C. Oxaloacetate, only
D. Lactate and acetyl-CoA
E. Pyruvate and oxaloacetate
Find out the competitive inhibitor for succinate dehydrogenase:
A. Malic Acid
B. Fumaric acid
*C. Malonic acid
D. Magnesium ion
E. Citric Acid
Amphybolic process must include intermediate metabolites which are involved in both anabolic and catabolic
pathways of a cell. Choose those one:
A. Malate-aspartate shuttle system
B. Hexose Monophosphate Shunt
C. Glycolysis
*D. All the proposed
E. Citric Acid Cycle
Name, please, the conversion of Krebs cycle regulated by inhibitor malonic acid
A. Succinyl-CoA-->succinate
B. Isocitrate--> alpha-ketoglutarate
*C. Succinate-->fumarate
D. Fumarate--> malate
E. Malate--> oxaloacetate
Krebs cycle does not occur in:
A. Heart
B. All the positions are right
*C. RBC
D. Liver
E. Skeletal Muscle
Choose, please, the transformation of intermediate metabolites of Krebs cycle required the function of multienzyme
complex:
*A. Alpha-ketoglutarate--> succinyl-CoA
B. Fumarate--> malate
C. Malate --> oxaloacetate
D. Citrate-->cis-aconitate
E. Isocitrate --> alpha-ketoglutarate
Energy production is due to catabolic pathways only. Name those one:
A. Fatty Acid Elongation
*B. Citric Acid Cycle
C. Hexose Monophosphate Shunt
D. Glycogenesis
E. Gluconeogenesis
Propose the correct continuation of the phrase: “Citric Acid Cycle is…”:
A. Placed in cytoplasm of a cell
*B. The main producer of reduced forms of coenzymes
C. Tissue respiration phase III
D. Anabolic process
E. The main producer of energy for erythrocytes
Name, please, the key metabolite, that may be formed in catabolic pathway both for glucose and palmitic acid in
aerobic condition, only:
A. Malate
*B. Acetyl-CoA
C. Pyruvate
D. Oxaloacetate
E. Lactate
The increase of one substrate concentration occurs the mitochondrial matrix during the inhibition of Citrate
synthetase in the Krebs Cycle. Find out this substrate:
*A. Acetyl ~ SCoA
B. Malate
C. Glucose
D. Alpha-Ketoglutarate
E. Fumarate
Name, please, the enzyme from Krebs cycle catalyzing the substrate phosphorylation:
A. Citrate synthase
B. Isocitrate dehydrogenase
C. Malate dehydrogenase
D. Fumarase
*E. Succinyl-CoA thiokinase
Name substances which are really terminal products for catabolic pathways and for human organism:
A. Carbon dioxide and Water
B. Bilirubin and Urea
*C. Uric acid and Urea
D. ATP and Carbon dioxide
E. Amino acids and Keto acids
How many stages are considered in catabolic pathway for glucose up to the terminal products (carbon dioxide and
water):
A. Two
B. Five
C. Four
*D. Three
E. One
The electrochemical potential formation occurs on the inner membrane of mitochondria during the active work of the
electron transport chain. Point the substance that can reduce the electrochemical potential value:
A. Succinate
B. Glucose
*C. 2,4-dinitrophenol
D. Citric acid
E. Malonic acid
Name, please the coefficient that can show the quantity of ATP molecules formed per one mole of oxidized organic
compound due to oxidative phosphorylation:
*A. P/O ratio
B. ADP/ATP ratio
C. The electrochemical potential
D. Protons gradient
E. Respiratory control
What type of tissue is specialized to carry out the oxidation uncoupled from phosphorylation?:
A. Erythrocytes of blood
B. Myocardium tissue
*C. Brown adipose tissue
D. Skeletal muscular tissue
E. White adipose tissue
Name, please, the substrate for Cytochrome oxidase (reduced form):
*A. Molecular oxygen
B. Isocitrate
C. Water molecule
D. Cytochrome C
E. Succinyl-CoA
The antibiotic oligomycin has been recently used in tuberculosis treatment. Point out the process in tuberculosis
bacillus that is inhibited by this drug:
A. Phagocytosis
B. The active transport of substances across membranes
C. Translation
*D. Oxidative phosphorylation
E. Anaerobic glycolysis
Carbon monoxide is discussed as the suppressor of tissue respiration in muscular tissue because of its ability to be
linked to:
A. Hemoglobin
B. Myoglobin
*C. All the positions are right
D. Cytochrome C oxidase
Name the component of electron transport chain that is not related to proteins but is also acceptor of protons and
electrons:
A. Cytochrome c oxidase
B. Cytochrome b
C. Cytochrome c
*D. CoQ
E. Cytochrome P[sub]450[/sub]
Name, please, the P/O ratio per one mole of pyruvate involved in oxidative decarboxylation if 1 mole of NADH is
formed in this reaction:
*A. Three
B. Five
C. Two
D. Four
E. Zero
Name, please, the enzyme system promoting the ADP/ATP maintenance both in the matrix of mitochondria and in
cytoplasma of the cell:
A. NADH-dehydrogenase
B. Cytochrome oxidase
*C. ATP/ADP translocase
D. ATP synthetase
E. Succinate dehydrogenase
Find out the property of uncoupler that helps it to penetrate across the inner membrane of mitochondria:
A. All the properties proposed
B. High solubility in water
C. High affinity to molecular oxygen
*D. High solubility in lipids
E. Very small shape of uncoupler molecule
Uncouplers of oxidative phosphorylation may be:
A. High levels of thyroid hormones
B. High levels of free fatty acids
*C. All the proposed
D. Thermogenins
E. High levels of serum bilirubin
Name, please, the acceptor of electrons from NADH-dehydrogenase in the electron transport chain:
A. Cytochrome c
B. CoQ
C. Cytochrome b
*D. Fe-S-proteins
E. Cytochrome oxidase
Acyl-CoA dehydrogenase involved in beta-oxidation of any Fatty Acid, has the prosthetic group FAD and is placed in
the inner membrane of mitochondria of cells where this process is in duration. How many moles of ATP may be
synthesized due to oxidative phosphorylation per 1 mole of acyl-CoA involved in Acyl-CoA dehydrogenase reaction?
A. Five
B. Four
C. One
*D. Two
E. Three
Antimycin A is discussed in scientific literature as the antibiotic whose pharmacological effects are based on its ability
to inhibit complex III of electron transport chain of the inner membrane of mitochondria. Choose the value for P/O
ratio of succinate oxidation in Krebs Cycle at the presence of antimycin A in mitochondria:
*A. Less then 2
B. _0
C. _3
D. Less then 3
E. _2
The complex I of electron transport chain may be inhibited by barbituric acid. Find out, please, the composition of this
complex:
A. FAD and Fe-S-proteins
B. Succinate dehydrogenase and Fe-S-proteins
*C. NADH-dehydrogenase and Fe-S-proteins
D. FMN and Fe-S-proteins
E. NAD and Fe-S-proteins
Choose, please, the P/O ratio per one mole of pyruvate involved in oxidative decarboxylation at the presence of
phenobarbital in high levels in the cell:
A. Three
B. Two
C. Five
D. Four
*E. Zero
Name, please, the factor that can block tissue respiration completely:
A. Valinomycin
B. Malonic acid
C. Oligomycin
D. Phenobarbital
*E. Potassium cyanide
Choose the enzyme of Krebs cycle that is considered as the part of Complex II of electron transport chain:
A. CoQ
*B. Succinate dehydrogenase
C. NaDH-dehydrogenase
D. Cytochrome oxidase
E. Cytochrome b, only
Name, please, the energy effect per one Krebs cycle due to oxidative phosphorylation:
A. 9 ATP
B. _1 GTP
*C. 11 ATP
D. 8 ATP
E. 12 ATP
Name, please, the inhibitor for complex IV of respiratory chain:
A. Hydrogen peroxide
B. Oxygen
C. Potassium chloride
D. Carbon dioxide
*E. Carbon monoxide
Choose, please, the value for ATP/ADP ratio at the moment when the tissue respiration has been just inhibited in the
cell:
A. ATP/ADP=0.5
B. ATP/ADP=0
*C. ATP/ADP>1,5
D. ATP/ADP=0.1
E. ATP/ADP=0.8
Name, please, the inhibitor for complex IV of electron transport chain:
A. Hydrogen peroxide
B. Carbon dioxide
*C. Hydrogen sulfide
D. Oxygen
E. Potassium chloride
The isocitrate is converted into alpha-ketoglutarate in the Krebs cycle. Choose the substance that can low the P/O
ratio for this reaction:
A. ADP
B. Citrate
C. Isocitrate dehydrogenase
*D. Antimycin A
E. NAD+
The tissue respiration is inhibited after coal gas poisoning. Point the electron transport chain enzyme whose activity
abruptly reduces in these conditions:
A. Succinate dehydrogenase
B. NADH-dehydrogenase
C. Cytochrome b1
D. Cytochrome c
*E. Cytochrome c oxidase
Choose, please, the P/O ratio per one mole of isocitrate involved in oxidative decarboxylation at the accumulation of
rotenone in the cell:
A. 2
B. P/O<2
C. P/O<3
*D. Zero
E. 3
Find out, please, the inhibitor for the complex III of electron transport chain in the inner membrane of mitochondria:
A. Barbituric acid
B. NADH
C. ATP
*D. Antimycin A
E. Rotenone
Rotenone (the inhibitor of the first complex of the electron transport chain) changes the P/O ratio for substrates that
are oxidized in Krebs Cycle. Choose the value of P/O at the presence of this inhibitor per 1 mole of malate that is
oxidized:
*A. Zero
B. <1
C. <3
D. <4
E. <2
Find out, please, the name of the third stage of tissue respiration:
A. The active transport of substances across membranes
B. Translation
C. Aerobic glycolysis
D. Oxidative phosphorylation
*E. Electron transport chain function
Name the terminal complex of respiratory chain:
A. Cytochrome C
*B. Cytochrome c oxidase
C. NADH-dehydrogenase and Fe-S-proteins
D. Cytochrome b, Fe-S-proteins and cytochrome C1
E. Succinate dehydrogenase
Find out the enzyme of electron transport chain that is transmembrane protein and may be considered as a pump for
protons from the matrix to the intra membrane space:
*A. Cytochrome C oxidase
B. Cytochrome b, only
C. Succinate dehydrogenase
D. CoQ
E. Cytochrome C
Choose, please, the P/O ratio per one mole of pyruvate involved in oxidative decarboxylation at the accumulation of
2,4-dinitrophenol in the cell:
A. Three
B. Four
*C. Zero
D. Two
E. Five
Which of the following inhibit complex IV of respiratory chain?
A. Antipyrine
B. Secobarbitone
*C. Cyanide
D. Amobarbital
E. Rotenone
Choose, please, the number of complexes in the long respiratory chain:
A. Two
*B. Three
C. Five
D. One
E. Four
Catalase activity is very important for cells where the accumulation of one toxic compound may be. Name, please,
this compound:
A. Nitric acid
B. Carbon monoxide
*C. Hydrogen peroxide
D. Potassium cyanide
E. Carbon dioxide
Name, please, the name of enzyme catalyzing the coupling of proton gradient use with the synthesis of ATP in
mitochondria:
A. Lipase
B. Pyruvate dehydrogenase
C. Monoaminooxidase
D. ATP/ADP-translocase
*E. ATP synthetase
ATP/ADP ratio equals 0.5 in the matrix of suspended mitochondria. What enzyme systems must be stimulated in the
matrix and inner membrane to increase this value up to 1?:
A. ATP/ADP-translocase
B. Citric Acid Cycle enzymes
*C. All the proposed
D. Electron transport Chain enzymes
E. ATP-synthetase
Cytochromes are:
A. Metal containing flavoproteins
*B. Iron-porphyrin proteins
C. Pyridine nucleotides
D. Peroxidases
E. Hemoglobin derivatives
Protons gradient in the inner membrane of mitochondria may be increased under condition of incorporation of high
doses of one vitamin in the body. Find out it:
A. Pantothenic acid
B. Cobalamin
C. Folic acid
D. Retinoic acid
*E. Ascorbic acid
Point out the location of the processes which take part in tissue respiration the most intensively:
A. EPR
B. Golgi complex
*C. Mitochondria
D. Lysosome
E. Cytoplasm
A patient is diagnosed with cardiac infarction. Blood test for cardio-specific enzymes activity was performed. Which
of enzymes has three isoforms?
A. Creatine kinase*
B. Aspartate transaminase
C. Alanine transaminase
D. Lactate dehydrogenase
E. Pyruvate kinase