Lesson 2, Module 1

Lesson 2, Module 1

The tertiary structure of protein is formed mainly due to disulfide bonds between side radicals of one amino acid, only. Point out it:

A. Cys --------B. Met

C. Asp

D. Lys

E. His

Primary structure of proteins is formed due to one type of bonds. Point out it:

A. Peptide bond -------------B. Disulfide bond

C. Ester bond

D. Hydrogen bond

E. Metal bond

Polypeptide chains of collagen include specific amino acids. Name one of them:

A. Hydroxyproline ------------------B. Formyl-methyonine

C. Cysteine

D. -alanine

E. Ornithine

There are many important protein functions in the human organism. Point out that of them, which isn't peculiar for proteins:

A. Catalyst

B. Transfer of substances

C. Antibody

D. Structural component of a cell

E. Solvent -----------------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. Elastin

B. Albumin

C. Myoglobin

D. Immunoglobulin

E. Pepsin

The proteins are able to carry out the regulatory function. Find out those proteins:

A. Aminopeptidase

B. Insulin --------------------C. Collagen

D. Hemoglobin

E. Immunoglobulin G

All proteins are divided into simple and conjugated ones. Find out the simple proteins among these ones:

A. Albumin of egg

B. Histone

C. Globulin of egg

D. Protamine ----------------------E. All the proteins above

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:

Quaternary

Tertiary Primary

Secondary

A conformation after limited proteolysis

Choose the factor that causes the sedimentation of protein in solution without denaturation:

Ammonia sulfate ------------Toluene

Sulfuric acid

Nitric acid

Sodium hydroxide

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:

lanine, Glycine

Asparagine, Glutamine

Arginine, Lysine --------------------Leucine, Valine

Tryptophan, Tyrosine

The mixture of proteins can be separated by salting-out. Specify the reagent formula that is used for this purpose:

HNO3NaCl ---------------H3PO4C2H5OH

C6H6Point out the type of bond allowing the formation of alpha-helix structure:

Ester bond between side chain radicals

Hydrogen bonds between peptide fragments --------------Disulfide bond between two cysteine radicals

Electrostatic interaction

Hydrogen bonds between side-chain radicals

Protein properties may be changed under the influence of some factors. Find out them:

Strong alkaline medium

Organic solvent

The temperature of the environment

Strong acidic medium

All the factors placed above -------------------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:

Disulfide bond

Hydrogen bond

Donor-acceptor bond

Electrostatic interaction

Hydrophobic interaction

The isoelectric point (I.P.) of a protein depends upon the amino acids composition of the protein. Choose the amino acid which high content decreases the I.P. value of protein:

lanine

Aspartic acid Histidine

Leucine

Tryptophan

Proteins are obligatory components of human diet. Specify the function of proteins in this case:

Nutritive

Transport

Regulatory

Structural

Catalytic

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:

CH3SH

CONH2OH --------------------NH2The 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:

pH=7.0

pH=7.6

pH=7.4

pH=5.0

pH=7.2

All are aromatic amino acids EXCEPT:

A. Phenylalanine

B. Tyrosine

C. Tryptophan

D. Lysine -----------------E. Positions A and D are correctNinhydrin 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-methionine

B. L-tyrosine

C. L-serine

D. L-proline ------------------------E. L-alanine

The content of these amino acids in the composition of acidic protein pepsin is too big in comparison with the content of others amino acids in it. Name them:

Lysine and Arginine

Valine and Leucine -------------------Aspartic acid and Glutamic acid Alanine and Glycine

Tyrosine and TryptophanThe 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-methionine

B. L-tyrosine -----------------------C. L-serine

D. L-proline

E. L-alanine

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?

Proline ---------------------Alanine

Glycine

Serine

Threonine

What type of amino acids mainly is represented as residues in proteins of human body?

L-(-amino acids

D-(-amino acids

D-(-amino acids

L-(-amino acids -------------------D-(-imino acids

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. Fibrous -------------------C. Stretch of beads

D. Planar

E. All of above

Which of the following bonds are intact during denaturation of proteins:A. Hydrophobic bonds

B. Hydrogen bonds

C. Peptide bonds -----------------D. Ionic bonds

E. All positions are correct

Alpha helix and Beta pleated sheet are examples of:

A. Primary structureB. Secondary structure ----------------------C. Tertiary structure

D. Quaternary structure

E. All positions are wrong

Biuret test is mainly done for:

Polysaccharides

Proteins -----------------------Lipids

DipeptidesAny of the above

Half saturation test using salting-out is done for:

Albumin

Globulin --------------------Fibrin

Prothrombin

Haemoglobin

What class of proteins Albumins and Globulins are related to?

A. Simple proteins ----------------------B. Glycoproteins

C. Chromoproteins

D. Metalloproteins

E. Lipoproteins

What physical-chemical properties are observed for fibrous protein only?

Solubility in water

Solubility in lipids

Amphoteric properties

Elasticity -------------------Denaturation and renaturation

Lesson 3 , Module 1

The conjugated protein necessarily contains special component as a non-protein part. Choose the substance that can't carry out this function:

Glucose

HNO3 ---------------------Fe 2+

Heme

Phosphate anion

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:

Dialysis

Paper chromatography

Ultracentrifugation ----------------Salting out

Spectrophotometry Point out a possible cause of hypoproteinemia:

Affected liver cells ----------------Multiple myeloma

Decreased permeability of the capillary wall

Overeating

Paraproteinemia

Point out a possible cause of hyperproteinemia

Increased permeability of the capillary wall

Infection (disturbed the macrophage system)-----Affected gastrointestinal tract

Nephritic syndrome

Diabetes mellitus

Which method is appropriate for the determination of total protein content in the blood serum:

Salting out

Foles test

Dialysis

Electrophoresis

Biuretic method -------------------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:

Low Density Lipoprotein

Albumin

Immunoglobulin

Hemoglobin -----------------Ceruloplasmin

What compound serves as non-protein part of glycoproteins:

Cu 2+Fe2+Galactose -----------------Heme

Phospholipid

Which group of proteins being phosphoproteins posses an activity but being dephosphorylated has lost the activity:

Hormones

Transfer of lipids

Transfer of vitamins

Enzymes -------------------Carriers through membrane

The conjugated protein necessarily contains special component as a non-protein part. Choose the substance that can't carry out this function:

Glucose

Salt of Hg2+ -------------------------Thiamine pyrophosphate

ATP

AMP

When the following amino acids are separated by running them on agarose gel, at pH 7 (electrophoresis method), which one of them will be slowest to the anodic end

Glycine

Valine

Aspartic acid

Lysine ----------------------Glutamic acid

Choose, please, the blood serum index used for estimation of hyperproteinemia state:

The total content of proteins ------------------The content of albumins

The content of acute phase proteins

The amino acid concentration

The total activity of all the enzymes

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:

Phosphoprotein

Nucleoprotein

Lipoprotein

Glycoprotein -----------------------Chromoprotein

It is in need to use the heme with iron ion for the active centers of cytochrome oxidase (the key enzyme of tissue respiration). Name the class of this conjugated protein:

Flavoproteins

Nucleoproteins

Lipoproteins

Glycoproteins

Chromoproteins -------------------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:

Optical activity

The big mass of the molecule

The ability of swelling

The high viscosity of the solution

The net charge of the molecule -----------------Albumins of blood plasma are negative charged under the condition of electrophoresis method duration. What electrode name have you to choose for albumins movement in the electric field?

Catode

Anode ---------------Silk electrode

Calomel electrode

Carbon electrode

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:

Flavoproteins

Nucleoproteins

Lipoproteins

Glycoproteins

Chromoproteins ----------------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:

Salting-out

Electrophoresis

Dialysis ---------------------Hydrolysis

Affine chromotography

The hormone receptors are related to the class of conjugated proteins. Name it:

Flavoproteins

Nucleoproteins ---------------Lipoproteins

Glycoproteins

Chromoproteins

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:

Nucleoproteins

Lipoproteins

Phosphoproteins -------------------Chromoproteins

Glycoproteins

All the proteins are divided into simple and conjugated ones. Find out the conjugated protein among these ones:

A. Egg albumin

B. Histone --------------C. Myoglobin

D. Protamine

E. Egg globulin

Name the location of deoxyribonucleoproteins in a cell, but not in the nucleus:

A. Lisosome

B. Cytoplasma

C. Mitochondria ---------------D. Microsome

E. Endoplasmic reticulum

Flavoproteins are usually catalysts in a cell due to the presence of special vitamin fragment in their structure. Name this vitamin:

A. Nicotin amide

B. Folic acid

C. Panthothenic acid

D. Riboflavin ---------------E. Ascorbic acid

Ceruloplasmin (the protein of blood plasma) contains copper ion and therefore has blue color. Name the class of this protein:

Metalloproteins -----------------Lipoproteins

Phosphoproteins

Chromoproteins

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:

Isoelectric point ------------------The mass of the molecule

The diameter of the molecule

The solubility in the water

The solubility in lipids

Ultracentrifugation is in need in biochemical investigations for:

The study of three-dimensional structure of the molecule

The separation of mixture from lo-molecular compounds -----------------The receiving of subcellular fractions of a cell

The investigation of chemical composition of organic compound

The determination of primary structure of proteins

Complex proteins do various functions. Find out the function of hemoglobin in erythrocytes:

Regulatory function

Catalytic function

Nutrition function

Transport function ---------------Protection against viruses

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:

Metalloproteins

Lipoproteins ---------------Phosphoproteins

Chromoproteins

Glycoproteins

Name the class of proteins used for the formation of ribosome subunits:

Flavoproteins

Lipoproteins

Phosphoproteins Ribonucleoproteins ---------------Glycoproteins

Toxic affection of liver results in dysfunction of protein synthesis. It is usually accompanied by the following kind of dysproteinemia:

Absolute hypoproteinemia*

Relative hypoproteinemia

Absolute hyperproteinemia

Relative hyperproteinemia

Paraproteinemia

Lesson 4 Module 1

Conjugated enzymes contain cofactors in their structure. Point out the location of vitamin derivative cofactor in the structure of enzyme:

Active centre -----------Allosteric centre

Hydrophobic fragment of structure

Hydrophilic fragment of structure

Near the metal-ion-cofactor in the structure

Only one factor can influence on the charge of amino acid radicals in the enzyme active centre. Name it:

Temperature

Pressure

pH medium --------------The presence of a competitive inhibitor

The surplus of a reaction product

One of the important properties of enzymes is their specificity of action. Check up a type of specificity for salivary amylase:

Absolute ----------------Absolute group

Absolute relative

Relative group

Stereochemical

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:

Apoenzyme

Coenzyme --------------Prosthetic group

Cofactor

Metall ions

The change of the temperature of environment from 0C to 38C can cause this effect:

The probability of enzyme-substrate complex formation is increased

A denaturation of enzymes occurs

The enzyme molecular charge changes

The substrate molecular charge changes

Enzyme action specificity varies

There are some factors influencing enzyme activity. Point out one of them resulting in complete loss of enzymatic activity:

Vitamin H

arbon dioxide

T = 100 C -------------------P =101325 Pa

Sodium chloride solution

There are some characteristic sites in the enzyme structure. Choose the most important site for enzyme function:

Allosteric centre

Active centre -----------------Cofactor

Apoenzyme

Catalytic site

Point out the factor that can cause the damage of enzyme function in a cell:

Temperature 37C

The presence of activator of enzyme

pH medium about 7.2

The presence of a product of enzymatic reaction

The surplus of protons in a cell ----------------Enzymes are the catalysts of protein nature. Name the property of enzymes which is not represented at the inorganic catalysts:

Ability to the denaturation -------------Wide specificity

Inert to chemical substrates

Big half-life

Ability to lowering the energy to activate the reaction

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:

Ascorbic acid

Nicotinamide

Riboflavin -----------------Biotin

Adenosine triphosphate

The enzyme hexokinase can catalyze the conversion of glucose or fructose in tissues. Find out the type of this enzyme specificity:

Absolute

Absolute group

Absolute relative

Relative group

Stereochemical

The catalytic site of active center of enzyme is used for:

Conversion of a substrate in the reaction ------Binding with the substrate

Binding with activator

Binding with inhibitor

Removal of a product of the reaction

There are different cofactors in the structure of conjugated enzymes but only one is used for transfer of amine group from amino acid to ketoacid. Name it:

Carboxybiotin

Pyridoxal phosphate

Thiamine pyrophosphate

FAD

NAD

Some terms are used for the description enzyme components. Point out the term of a protein part of conjugated enzyme:

A. Apoenzyme --------------B. Coenzyme

C. Prosthetic group

D. Cofactor

E. Metall ions

Oxidoreductase can contain prosthetic group with vitamin B2. Name it:

A. Retinal

B. Flavin adenine dinucleotide (FAD) -----------C. Nicotinamide adenine dinucleotide (NAD)

D. Pyridoxal phosphate

E. Ascorbic acid

A substrate molecule is destructed upon enzyme action, and the water is used for the products structure formation. Name the enzyme class:

A. Oxidoreductase

B. Hydrolase --------------C. Lyase

D. Ligase

E. Isomerase

A qualitative composition of product molecule is completely identical to substrate one, but the structure is different. Name the enzyme class:

A. Oxidoreductase

B. Hydrolase

C. Lyase

D. Ligase

E. Isomerase ----------------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 dephosphorylation

B. ATP is used for a substrate phosphorylation

C. ATP is used for hydrolysis of a substrate bond

D. ATP is used for the new bond formation during the interaction of two substrates ---------------E. ATP is used for a substrate decarboxylation.

Coenzyme forms are correctly matched to vitamins except one. Point out it:

A. Biotin carboxylated biotin

B. Vitamin B1 - ATP --------------C. Niacin NAD+ + NADP+

D. Vitamin B2 FMN + FAD

E. Pantothenic acid CoASH

Enzymes mediating transfer of a structural fragment from one molecule to another are:Transferases --------------------OxidasesLyases

Peptidases

Ligases

Which bond is cleaved by Alpha amylase in oral cavity?

Alpha 1-4 glycosidic ------------------Alpha 1-6 glycosidicBeta 1-4 glycosidicBeta 1-6 glycosidic

Ester bond in any ester structureWhich of the following is the reaction that is catalyzed by lyase:

Dehydration

Oxidation

Oxidative decarboxylation

Hydrolysis --------------Acetylation

All biological catalysts are not proteins This statement is justified by this notion:

All enzymes do not follow the Michaelis Menten hypothesis

RNAs can act as ribozymes --------------Antibodies take part in the catalysis of many reactions

Metal ions are involved in attachment to enzymes

Enzyme activity may be controlled by hormones

LDH1 and LDH2 levels are raised in the following organ damage

Heart, RBC, kidney ----------------------Heart, kidney, liver

Liver, brain, kidney

Brain, heart, liver

Brain, bones, liver

Name, please, the principle base used for the classification of enzymes:

Type of chemical reaction catalyzed by enzyme ---------Chemical structure of enzyme

Type of energy conversion

Chemical structure of non-protein part of the enzyme

Chemical structure of products for enzymatic reaction

Name the vitamins whose derivatives are used for the formation of oxidoreductase structure:

B2, B3B6, B9C, P

A, E

H, D

Chymotrypsin is the proteolytic enzyme catalyzing the cleavage of peptide bonds in any protein molecule. Name the class of this enzyme:Oxidoreductase

Isomerase Lyase

Ligase

Hydrolase --------------------The active centre of simple enzyme is composed from:

The cofactor and prosthetic group

Linear fragment of polypeptide chain

Some amino acid residues of polypeptide chain placed in the same spatial fragment -----------------One polypeptide chain completely

The terminal amino acid residues

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. Ligase

C. Lyase

D. Hydrolase -------------E. Oxido reductase

The relative group specificity may be found for enzymes catalyzing the digestion of proteins in GIT. Find out their trivial name:

Protein kinase ---------------Protein phosphatase

Peptidase

Transaminase

Urease

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?

They have the same molecular weight

They catalyze the same reaction*

The same tissue localization

The same electrophoretic mobility

The same net charge of the molecule

In case of enterobiasis acrihine - the structural analogue of vitamin B2 - is administered. The synthesis disorder of which enzymes does this medicine cause in microorganisms?

FAD-dependent dehydrogenases -----------------Cytochromeoxidases

Peptidases

NAD-dependet dehydrogenases

Aminotransferases

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 oxidation-reduction reactions due to the buildup of pseudo-coenzyme:

FMN

NAD

CoQ

FAD

TDP

Lesson 5 Module 1

.

E. Fisher`s theory explains the mechanism of enzyme action with the fixed type of specificity, only. Name it:

A. Absolute --------------B. Absolute group

C. Absolute relative

D. Relative group

E. Stereochemical

There are some factors influencing enzyme activity. Point out one of them resulting in complete loss of enzymatic activity:

A. Vitamin H

B. Oxygen

C. t0 C = 1000 C ----------------D. P =101325 Pa

E. Sodium chloride solution

Choose the factor that changes the cytoplasmic enzyme conformation mainly:

A. Suicide inhibitor

B. Environmental pH value about 7.4

C. Environmental temperature value about 250 C

D. Allosteric inhibitor -------------------E. WaterPoint out the way of proenzyme transformation to the active enzyme:

A. Limited proteolysis -----------------B. Dehydration

C. Decarboxylation

D. Inhibitor action

E. Vitamin non-protein part dissociation from enzyme Competitive inhibitor always interacts with enzyme active centre. Find out the explanation of this phenomenon:

A. Inhibitor causes the denaturation of active centre

B. Inhibitor is similar to a substrate structure -----------C. Inhibitor is an exact copy of a substrate structure

D. Inhibitor is similar to the product's structure

E. Inhibitor forms a covalent type of bonds with amino acid residues of active centreCovalent modification of inactive form of enzyme may be catalyzed by special enzyme in a cell. Name it:

A. Esterase

B. Ligase

C. Protein kinase ---------------- D. Hydroxylase

E. Oxygenase

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:

Allosteric

Competitive ----------------Non-competitive

Dephosphorylation

Limited proteolysis

Choose the name of scientists whose experiments are recognized as the basis in understanding of induced fit theory for mechanism of enzymatic reaction:

Michaelis L.

Menten M.

Koshland D. ----------------Fisher E.

Haldane R.

Diisopropyl phosphofluoride (DFP) reacts with serine proteases irreversibly and therefore is:

Allosteric inhibitor ---------------Non-competitive inhibitor

Competitive inhibitor

Affinity label inhibitorA stimulator

The common feature of an enzyme-cascade system regulation is:

A. Feed back inhibition --------------B. Competitive inhibition

C. Counter-regulationD. Amplification

E. Suicide inhibition

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. Peptide bond

B. Hydrophobic interaction

C. Hydrogen bond

D. Donor-acceptor bond

E. Electrostatic interaction --------------The common enzymatic reaction may be represented so: E + S ES ESEP 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, only

B. The concentration of enzyme, only

C. The concentration of a substrate, enzyme and product, only

D. The concentration of enzyme-substrate complex, only

E. The concentration of a substrate, enzyme, product and stability of ES-complex --------------Heme synthesis starts from glycine and succinyl-SCoA interaction with -aminolevulinate synthetase help. It is inhibited by the terminal metabolic product - heme. Name the inhibition type:

A. Competitive Inhibition

B. Uncompetitive Inhibition

C. Non-competitive Inhibition

D. Limited proteolysis

E. Feedback Inhibition-------------The inhibitor influence on the enzymatic reaction rate is investigated. The graph dependences V - [S] without the inhibitor (1) and at the presence of the inhibitor (2) are constructed.

Name the type of the inhibitor:

A. Competitive

B. Non-competitive ---------------C. Uncompetitive

D. Allosteric

E. Complete

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. Limited proteolysis

B. Allosteric regulation ------------------------C. Activation by Ca2+D. The change of pH medium

E. Competitive inhibition

Covalent catalysis as mechanism of enzyme catalysis was studied in experimental works with one proteolytic enzyme. Find out it:

A. Pepsin

B. Aldolase

C. Chymotrypsin ----------------D. Decarboxylase

E. Glucoisomerase

Suicide type of inhibition is considered when:

A. The inhibitor structure is similar to substrate one

B. The product of reaction is the allosteric inhibitor for enzyme

C. There is the intermediate metabolite formation from the inhibitor which tightly binds to the active centre of enzyme to block it ----------D. The end-product of reaction binds to the structure of the substrate to give non-soluble complex

E. The end-product of reaction is not removed from the environment

Choose the method that is more often used for the determination of inhibitor type:

A. Nuclear magnetic resonance method

B. Michaelis-Menten graphical method

C. Briggs-Haldane graphical method

D. Lineweaver-Burk graphical method------------E. Eadie-Hofstee graphical method

Find out the irreversible type of enzyme inhibition:

A. Competitive

B. Noncompetitive

C. Uncompetitive

D. Allosteric

E. Suicide ---------------Point out the activator used for the determination of amylase activity:

A. CuSO4B. NaCl ---------------C. H3PO4D. ATP

E. Ca2+ The majority of key enzymes contain the allosteric centre. Specify a role of this centre:

A. It attaches the substrate ----------B. It attaches the regulatory factor

C. It changes the structure of the substrate

D. It promotes the dissociation of a coenzyme

E. It blocks the active centre

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. Covalent modification----------------------C. Activation by Ca2+D. The change of pH medium

E. Competitive inhibition

Sulfonamides are used as drugs to protect our organism from some 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. Noncompetitive

C. Uncompetitive

D. Allosteric

E. Suicide

Name, please, the inhibitor for salivary amylase:

A. Copper sulfate ----------------- B. Sodium chloride

C. Potassium cyanide

D. Alanine

E. Hydrogen peroxide

Name the kinetic index that is changed under the influence of competitive inhibitor on enzyme:

A. Michaelis constant

B. The initial velocity of enzymatic reaction ----- C. The maximal velocity of enzymatic reaction

D. The dissociation constant of enzyme-substrate complex (ES)

E. The rate constant for the formation of ES

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:

The temperature of environment

The pH of environment ------------------The addition of competitive inhibitor to the environment

The addition of activator to the environment

All the factors proposed may be in need

The affinity of enzyme molecule to substrate one may be estimated using the value of:

pH of the environment

The temperature

Km for the enzyme -----------------Vmax for reaction duration

The initial velocity of the reaction

Name, please, the equation for V-[S] dependence for the moment of complete saturation of all the active centers of enzyme molecules:

V=Vmax[S]/Km+[S] ----------V= kVmax

V=Vmax/Km+[S]

V=Vmax

V=k [S]

Cholesterol synthesis is regulated by feed-back mechanism. Name the allosteric inhibitor of key enzyme for this synthesis:

ATP

Cholesterol --------------Glucose

ADP

NADPH

Salivary amylase activity may be decreased by:

The change of pH from 6,8 to the value 5,5

The decrease of temperature from 38C to 25C

The addition of copper sulfate

The increase of temperature from 38C to 65C

All the changes described may be in need --------------Name, please, the factors that must be in constant levels during the investigation of enzyme concentration influence the velocity of enzymatic reaction:

pH of the environment The temperature

Substrate concentration

Activator concentration

All the factors proposed must be in constant levels -------Lesson 6 Module 1

Point out the activator, used for the determination of urine amylase activity under Volgemut's method:

A. CuSO4B. NaCl ----------C. H3PO4D. ATP

E. Ca2+Patient's amylase activity in the urine excesses the normal values in ten times as much. Point out the possible diagnosis:

A. Viral hepatitis

B. Diabetes mellitus

C. Sharp pancreatitis ---------------D. Influenza

E. Angina

Find out the term for unit of enzyme activity that is estimated as the number of molecules of a substrate catalyzed upon in a period 1 second by a single enzyme molecule:

A. Total activity

B. Specific activity

C. Turnover number

D. Katal ----------------E. The Unit of an enzyme activity

Find out the substrate used for amylase activity determination in the urine of patient:

A. Glucose

B. Pyruvate

C. Maltose

D. Glycogen

E. Starch ---------------Find out the method for separation of isozymes to determine their content in the blood serum of patient:

A. Dialysis

B. Electrophoresis ---------------C. Spectrophotometry

D. Gel chromotography

E. Salting-out

There is the treatment of patients with achlorhydria (the absence of free hydrochloric acid in the gastric juice of patient) by enzyme as a drug. Name it:

A. Rennin

B. Pyruvate

C. Pepsin -------------------D. Trypsin

E. Chymotrypsin

Choose the enzyme used as diagnostic reagent for glucose content determination in the blood:

A. Glucose-6-phosphatase

B. Pyruvate kinase

C. Maltase

D. Glucose oxidase --------------E. Amylase

A lot of factors must be taken into account to promote methodic requirements for the determination of the enzyme activity in biological fluids. Choose, please, the most important from them:

A. pH of the environment

B. Temperature of the environment

C. Substrate concentration

D. Enzyme concentration

E. All the positions placed above ---------------The determination of Lactate dehydrogenase (LDH) isozymes content showed the increase of LDH4 and LDH5 fractions in the patient's blood plasma. Point out the presumable diagnosis:

A. Viral hepatitis

B. Skeletal muscle dystrophy -----------------C. Diabetes mellitus

D. Myocardial infarction

E. Acute pancreatitis

Name, please, the reagent that is added to urine of patient to increase the activity of amylase:

A. Sodium phosphate

B. Sodium chloride ------------------C. Copper sulfate D. Glucose

E. Choline

Name the unit of the enzyme activity, if the reaction is carried out by the quantity of the enzyme at a rate of 1 mol of the substrate conversion per second:

A. Standard international unit

B. Katal -------------------C. Specific activity

D. Turnover number

E. Conditional unit of activity

Patient's amylase activity in the urine equals 16 units. Point out the possible state for this patient:

A. There is viral hepatitis in patient

B. There is diabetes mellitus in patient

C. There is the sharp pancreatitis in patient

D. The patient is apparently healthy ------------E. There is Angina in patient

Find out the term for unit of enzyme activity that is estimated as the number of molecules of a substrate acted upon in a period 1 second by a single enzyme molecule:

A. Total activity

B. Special activity

C. Turnover number

D. Katal -------------------E. Unit of an enzyme activity

Pancreatine is proposed as the drug to promote the normal digestion of proteins in the small intestine of patients with chronic pancreatitis. Choose the enzyme that is the component of this drug and is possible to destroy protein structure:

A. Amylase

B. Lipase

C. Pepsin

D. Trypsin -----------------E. Maltase

Competitive inhibitors of enzymes may be used as drugs. Try to find out the medicine that is used to decrease the rate of folic acid synthesis from para-aminobenzoic acid in microorganisms which can cause the inflammation state of tissues in humans:

A. Antimycin A

B. Pancreatine

C. Phenobarbital

D. Sulfonamide -------------------------E. Phosphogluconate

Enzyme deficiency in patient usually is discussed as severe form of pathology because:

A. It is genetic disorder that is difficult to treat --B. It is secondary reason of pathology

C. It is difficult to determine it

D. It cannot be prevented in the prenatal period of organism development

E. It can be discovered in adults, only

We cannot use the enzymes as medicines for oral administration because oral dose of enzyme:

A. Causes the allergic reactions in human organism

B. Stimulates the production of albumins by the liver

C. Can lead to the cleavage of blood plasma proteins

D. Is digested in gastrointestinal tract ------------E. Changes the acid-alkaline balance in the blood

The decrease of Choline esterase activity in the blood serum of patient is the signal to care for the function of one organ mainly. Name it:

A. Liver ------------------B. Spleen

C. Brain D. Kidney

E. Pancreas gland

The principle of the method for Choline esterase activity determination is based on the ability of the product for the reaction catalyzed by this enzyme to change the pH of the incubation phase. Try to give the name of this product:

A. Choline

B. Serum Albumin

C. Acetyl choline

D. Phosphatidyl choline

E. Acetic acid -------------------Genetic disorder associated with enzymatic pathology may be caused by the:

A. Deficiency of the non-protein part of enzyme, only

B. Disorder in the regulation of the transcription of mRNA for enzyme synthesis ---------------C. The damage of the feed-back mechanism of enzyme regulation

D. Super-activation of inducer synthesis that is used to stimulate transcription of mRNA for enzyme

E. All the reasons described are right

Find out, please, the value for amylase activity in the urine (Volgemut`s method) corresponding the pathological state - acute pancreatitis:

16 units

2 units

160 units ------------------32 units

8 units

Find out the type of Lactate dehydrogenase (LDH) isozymes whose activity is in high level in the blood plasma of patients at myocardium infarction:

LDH4 and LDH5LDH3, only

LDH2 and LDH3LDH1, only ------------------LDH5, only

The Acidic Phosphatase activity is determined in the blood serum of patients with this pathologic state. Name it:

Atherosclerosis of blood vessels

Myocardium infarction

Prostatitis -------------------Acute pancreatitis

Renal insufficiency

Point out the proteolytic enzyme of the blood that helps to solvate the fibrin clot:

A. Plasminogen

B. Lysokinase

C. Plasmin -------------------D. Antifibrinolysinogen

E. Thromboplastin

Profuse foam appeared when dentist put hydrogen peroxide on the mucous of the oral cavity. What enzyme caused such activity?

Catalase*

Cholinesterase

Acetyltransferase

Glucose-6-phosphatdehydrogenase

Methemoglobinreductase

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?

Myocardium infarction *

Viral hepatitis

Collagenosis

Diabetes mellitus

Diabetes insipidus

Marked increase of activity of -forms of CPK (creatine phosphokinase) and LDH-1 were revealed on the examination of the patient's blood. What is the most likely pathology?

Miocardial infarction*

Hepatitis

Rheumatism

Pancreatitis

Cholecystitis

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?

In the heart muscle (initial stage of myocardium infarction)*

In skeletal muscles (dystrophy, atrophy)

In kidneys and adrenals

In connective tissue

In liver and kidneys

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?

Superoxide dismutase*

Catalase

Peroxidase

Glutathione peroxidase

Glutathione reductase

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. LDH4B. LDH1*

C. LDH5D. LDH3E. LDH2 Lesson 7, Module 1

Nucleoside triphosphate is formed in Krebs Cycle. Point out its abbreviation:

A. ATP

B. CTP

C. GTP ----------------D. UTP

E. TTP

Only one dehydrogenase of Krebs Cycle has the non-protein part FAD. Name it:

A. Isocitrate dehydrogenase

B. -Ketoglutarate dehydrogenase

C. Malate dehydrogenase

D. Succinate dehydrogenase --------------E. Pyruvate dehydrogenase

Vitamin B1 (coenzyme TPP) is necessary for only one dehydrogenase function in Krebs Cycle. Point out it:

A. Malate dehydrogenase

B. -Ketoglutarate dehydrogenase -----------C. Isocitrate dehydrogenase

D. Succinate dehydrogenase

E. Lactate dehydrogenase

Two reactions of Krebs Cycle are named as oxidative decarboxylation. Point out the enzyme for this type of reaction:

A. Citrate synthase

B. cis-Aconitate hydratase

C. Isocitrate dehydrogenase -------------------D. Succinate dehydrogenase

E. Succinyl~SCoA synthase

Name, please, the class of organic compound usually used as energy source for anabolic pathways in humans:

A. Monosaccharides

B. Alcohols

C. Carboxylic acids

D. Nucleosides

E. Nucleoside triphosphates -------------Name, please, the process that is considered as the second phase of catabolic pathways in humans:

A. Gluconeogenesis

B. Glycolysis --------------C. Urea cycle

D. Krebs cycle

E. Proteolysis

Choose, please, the transformation of intermediate metabolites of Krebs cycle required the function of multienzyme complex:

A. Citratecis-aconitate

B. Malate oxaloacetate

C. Isocitrate alpha-ketoglutarate

D. Alpha-ketoglutarate succinyl-CoA ----------E. Fumarate malate

Name, please, the conversion of Krebs cycle regulated by inhibitor malonic acid

A. Succinyl-CoAsuccinate

B. Malate oxaloacetate

C. Isocitrate alpha-ketoglutarate

D. Succinatefumarate --------------E. Fumarate malate

Find out, please, the enzyme whose activity is inhibited under the accumulation of ATP in the matrix of mitochondria:

A. Aconitase

B. Malate dehydrogenase

C. Citrate synthase --------------D. Alpha-ketoglutarate dehydrogenase

E. Fumarase

How many stages are considered in catabolic pathway for glucose up to the terminal products (carbon dioxide and water):

A. Two

B. Three -------------C. One

D. Four

E. Five

Name, please, the key metabolite that may be formed in catabolic pathway both for glucose and palmitic acid in aerobic condition, only:

A. Pyruvate

B. Oxaloacetate

C. Acetyl-CoA -----------------D. Lactate

E. Malate

Name, please, the process that is anabolic pathway in human organism:

A. Gluconeogenesis ----------------B. Glycolysis

C. Fatty Acid Oxidation

D. Krebs cycle

E. All the proposed

Name, please, the initial substrates for Krebs cycle (first reaction):

A. Pyruvate and oxaloacetate B. Oxaloacetate, only

C. Acetyl-CoA and oxaloacetate ---------------D. Lactate and acetyl-CoA

E. Citric acid, only

Mg2+ and Mn2+ are in need for the function of one enzyme from this register, only. Point out it:

A. Succinate dehydrogenase

B. Malate dehydrogenase

C. Isocitrate dehydrogenase ------------D. Aconitase

E. Fumarase

Find out the competitive inhibitor for succinate dehydrogenase:

Malonic acid --------------Malic Acid

Fumaric acid

Citric Acid

Magnesium ion

Krebs cycle does not occur in:

Skeletal Muscle

Heart

RBC -------------Liver

All the above

Fluroacetate inhibits:

Citrate synthetase

Cis-Aconitase ------------------Succinate dehydrogenase

Alpha-ketoglutarate dehydrogenase

All these metabolic pathways or processes take place inside the mitochondria except:

Glycolysis

Krebs cycle

Urea cycle

Oxidative phosphorylation

Fatty acid -oxidation ----------------Number of NADH molecules produced in Citric Acid Cycle is:

2

3 ----------------------4

5

6

Name substances which are really terminal products for catabolic pathways and for human organism:

Uric acid and Urea -------------------Carbon dioxide and Water

ATP and Carbon dioxide

A mino acids and Keto-acids

Bilirubin and Urea

Exogenous substances may be involved in catabolic pathways to be used as energy sources for humans EXCEPT:

Vitamins

Monosaccharides

Amino acids

Fatty acids

Alcohols -----------------------The accumulation of NADH in the matrix of mitochondria is the signal to inhibit:

Citrate lyase

Cis-Aconitase

Isocitrate dehydrogenase -----------------Fumarase

Malate dehydrogenase

Amphybolic process must include intermediate metabolites which are involved in both anabolic and catabolic pathways of a cell. Choose those one:

Glycolysis

Hexose Monophosphate Shunt

Citric Acid Cycle ----------------Malate-aspartate shuttle system

All the proposed

Energy production is due to catabolic pathways only. Name those one:

Gluconeogenesis

Citric Acid Cycle ---------------Fatty Acid Elongation

Hexose Monophosphate Shunt

Glycogenesis

Propose the correct continuation of the phrase: Citric Acid Cycle is:

The main producer of reduced forms of coenzymes

Anabolic process

Placed in cytoplasm of a cell

The main producer of energy for erythrocytes

Tissue respiration phase III -----------------How many moles of high energy bond containing compound are produced due to substrate phosphorylation in one round of Citric Acid Cycle:

Twelve ----------------Two

One

Three

Four

The rate limited step for Citric Acid Cycle duration is the reaction catalyzed by:

Citrate synthase

Cis-Aconitase

Isocitrate dehydrogenase

Alpa-ketoglutarate dehydrogenase

Malate dehydrogenase

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:

Citrate is converted to Cis-Aconitate

Isocitrate is converted to Alpa-ketoglutarate

Alpa-ketoglutarate is converted to Succinyl-CoA ---------Malate is converted to Oxaloacetate

Succinate is converted to Fumarate

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:

Citrate synthase

Cis-Aconitase

Isocitrate dehydrogenase ----------------------Alpa-ketoglutarate dehydrogenase

Succinate dehydrogenase

Krebs Cycle is the stage of catabolic ways in the organism. Point, please, the number of stage, which is corresponded to Krebs Cycle:

1

2

4

3 ----------------------------5

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:

0.5 --------------------1

3

2.5

5

Isocitrate was used as an oxidized substrate in the experiment with isolated mitochondria. Specify the substance that can inhibit the isocitrate oxidative decarboxylation:

ADP

Glucose

ATP --------------------Citrate

cAMP

Name, please, the enzyme from Krebs cycle catalyzing the substrate phosphorylation:

. Succinyl-CoA thiokinase ----------------------. Fumarase

. Isocitrate dehydrogenase

D. Malate dehydrogenase

. Citrate synthase

The increase of one substrate concentration occurs the mitochondrial matrix during the inhibition of Citrate synthetase in the Krebs Cycle. Find out this substrate:

. Glucose

. Acetyl ~ SCoA --------------------------------. (-Ketoglutarate

D. Malate

. Fumarate

Lesson 8, Module 1

Name, please, the inhibitor for complex IV of electron transport chain:

Carbon dioxide

Potassium chloride

Hydrogen peroxide

Hydrogen sulfide ----------------Oxygen

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:

.