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THE MINISTRY OF HEALTH OF UKRAINE
ZAPOROZHYE STATE MEDICAL UNIVERSITY
BIOCHEMISTRY & LABORATORY DIAGNOSTICS DEPARTMENT
TEST EXERCISES FOR TRAINING
A course of Biochemistry for students of Medical
Department
ZAPOROZHYE
2012
The Central Methodical Commission of the Medical University has discussed and recommended
these test exercises for teach students on biochemistry at the Medical Department (the second year
of study).
These test exercises were translated from Russian. They are used at each lesson for the
independent work of students.
The book consists of blocks of tests for each lesson and contains answers to each test.
Editors: PhD, professor Aleksandrova K.V.
PhD, ass. professor Krisanova N.V.
PhD, ass. professor Makoed O.B.
PhD, as. pr. Rudko N.P.
A Translation: Krisanova N.V.
Yechina N.D.
Belitskaya L.M.
LESSON 1
THEME: AMINO ACIDS AND PEPTIDES. COLOUR REACTIONS TO AMINO ACIDS.
1. The amino acids mixture is obtained after protein digestion. Call the quality reaction that proves
the arginine presence:
A. Biuret reaction
B. Xantoprotein reaction
C. Fole's reaction
D. Nitroprusside reaction
E. Sakaguchi reaction
2. Each L-amino acid has its isoelectric point (I.P.). Choose the pH region for histidine I.P.
A. pH=1,0-4,0
B. 5<pH<7
C. pH=7,0
D. 7<pH<9
E. pH>10
3. Point out from these amino acids the diamino monocarboxylic one:
A. Trp
B. Ser
C. Asp
D. Arg
E. Ala
4. The amino acids mixture was formed after protein hydrolysis. Point out the qualitative reaction,
which proves the presence of cysteine:
A. Biuret reaction
B. Xantoprotein reaction
C. Fole's reaction
D. Millon's reaction
E. Sakaguchi reaction
5. Each L-amino acid has its own isoelectric point (I.P.). Identify the area of I.P. for Asp:
A. pH=1,0-4,0
B. 5<pH<7
C. pH=7,0
D. 7<pH<9
E. pH>10
6. The amino acid's reaction with nitroprusside reagent gives the positive effect. Name this amino
acid:
A. Phe
B. Pro
C. Cys
D. Met
E. Asp
7. The chromatogram for five amino acids (Phe, Asp, Trp, Val, Tyr) was obtained by method of a
thinlayered chromatography on paper in separation mixture (butanol: acetic acid: water). Name
the amino acid, which remained on the start line:
A. Phe
B. Val
C. Tyr
D. Trp
E. Asp
8. Choose the amino acid, which can't attach to other one by usual peptide fragment -NH-CO- :
A. Phe
B. Pro
C. Cys
D. Met
E. Asp
9. Point out the amino acid that is described as: diamino monocarboxylic, acyclic, particularly
essential:
A. Tyr
B. Val
C. Lys
D. Pro
E. Asp
10. Choose the amino acid that will take place in the anode fraction after electrophoresis (pH=7,0)
A. Phe
B. Met
C. Gly
D. Arg
E. Asp
LESSON 2
THEME: PROTEIN STRUCTURE. PHYSICAL AND CHEMICAL PROPERTIES OF PROTEINS.
PROTEIN CLASSIFICATION. SIMPLE PROTEINS
1. The reason of damage of a-helix formation in polypeptide chain may be the large concentration
(> 30 %) of one amino acid. Name it:
A. Asp
B. Pro
C. Tyr
D. Ser
E. Gly
2. The tertiary structure of protein is formed thanks to disulfide bonds between side radicals of only
one amino acid. Point out it:
A. Cys
B. Met
C. Asp
D. Lys
E. His
3. Primary structure of proteins is formed thanks to one type of bonds. Point out it:
A. Peptide bond
B. Disulfide bond
C. Ester bond
D. Hydrogen bond
E. Metal bond
4. The polypeptide chain can keep about 1000 of amino acid residues. Point out the minimal
quantity of amino acid residues in the chain allowing the formation of the a-helix:
A. 10
B. 40
C. 15
D. 20
E. 3
5. Polypeptide chains of collagen include specific amino acids. Name one of them:
A. Hydroxyproline
B. Formyl-methyonine
C. Cysteine
D. b-alanine
E. Ornithine
6. There are not enough proteins with formed b-pleated sheet structure in nature. Name one of
them:
A. Albumin
B. a-Keratin of hair
C. Fibroin of a silk
D. Elastin of cartilages
E. Protamine of plants
7. 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
E. Solvent
8. The solubility of proteins in saline solutions is determined by their native structure. Point out the
protein, which will only swell in saline solution:
A. Elastin
B. Albumin
C. Myoglobin
D. Hemoglobin
E. Pepsin
9. Blood plasma proteins are able to carry out the regulative function. Check up these proteins:
A. Enzymes
B. Hormones
C. Receptors
D. Structural elements
E. Antibody
10. All proteins are divided into simple and conjugated ones. Find out the conjugated protein among
these ones:
A. Albumin of egg
B. Histone
C. Hemoglobin
D. Protamine
E. Globulin of egg
LESSON 3
THEME: CONJUGATED PROTEINS. NUCLEIC ACIDS.
1. Name the authors of DNA secondary structure:
A. Nirenberg, Ochoa
B. Michaelis, Menten
C. Watson, Crick
D. Jakob, Monod
E. Meselson, Stal
2. Point out constituents of nucleoside:
A. Pentose, H3PO4
B. Nitrogenous base, H3PO4
C. Pentose, H4P2O7
D. Nitrogenous base, pentose
E. Nitrogenous base, H4P2O7
3. Point out the location of DNA in the cell, except nucleus:
A. Lysosome
B. Cytoplasm
C. Mitochondria
D. Microsome
E. Endoplasmic reticulum
4. Point out the type of the bond, which stabilizes the primary structure of nucleic acid:
A. Hydrogen
B. Disulfide
C. Peptide
D. Phosphodiester
E. Van der Waal's forces
5. Choose the proteins, which are included into the deoxyribonucleoprotein (DNP) structure of
eukaryotic cells:
A. Albumins
B. Globulins
C. Histones
D. Collagen
E. Glutelines
6. Point out bonds that stabilize the DNA double helix and are formed between the complementary
pairs of bases:
A. Phosphodiester
B. Hydrophobic
C. Hydrogen
D. Peptide
E. Disulfide
7. Nucleic acids have acid properties due to the presence of residues in their structure:
A. Adenosine
B. Guanine
C. Deoxyribose
D. Ribose
E. Phosphoric acid
8. Point out the physiological role of tRNA minority bases:
A. Are not important physiologically
B. Casual components
C. Protection the RNA molecule from enzymatic split- ting
D. Take part in translation
E. Form the promotor structure
9. Choose the qualitative reaction on carbohydrates of nucleic acids:
A. Millon reaction
B. Molybdenic test
C. Biuret reaction
D. Barfed reaction
E. Diphenylamine test
10. Deoxyribose differes from ribose by:
A. The presence of hydroxyl-group at the second carbon atom
B. The absence of hydroxyl-group at the second carbon atom
C. The quantity of carbon atoms
D. The presence of amino group
E. The presence of hydroxyl-group at the third carbon atom
LESSON 4
THEME: ENZYMES STRUCTURE . GENERAL PROPERTIES OF ENZYMES. A
CLASSIFICATION OF ENZYMES.
1. Enzymes are the catalysts of protein nature. Name the property of enzymes which is not
presented at the inorganic catalysts:
A. Ability to the denaturation
B. Wide specificity
C. Inert to chemical substrates
D. Big half-life
E. Ability to lowering the energy to activate the reaction
2. One of the important properties of enzymes is their specificity of action. Check up a type of
specificity for amylase:
A. Absolute
B. Absolute group
C. Absolute relative
D. Relative group
E. Stereochemical
3. Some terms are used for the description of non-protein part of an enzyme. Point out the term of
non-protein part that easily dissociates from polypeptide chain:
A. Apoenzyme
B. Coenzyme
C. Prosthetic group
D. Cofactor
E. Metall ions
4. 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
5. The change of the temperature of invironment from 00 C to 400 C can cause this effect:
A. The probability of ES complex formation is increased
B. A denaturation of enzymes occurs
C. The enzyme molecular charge changes
D. The substrate molecular charge changes
E. Enzyme action specificity varies
6. The optimum pH for cytoplasm enzymes activity varies from 7,2 to 7,6. Point out all possible
changes in active centre structure of such enzyme at pH=7,0:
A. Changes are not presented
B. Radicals of amino acids get negative charge
C. Neutralization of negatively charged radicals
D. Formation of ester bonds between radicals
E. Destruction of the active centre
7. A substrate molecule is destructed upon enzyme action, and the water is used for the product's
structure formation. Name the enzyme class:
A. Oxidoreductase
B. Hydrolase
C. Lyase
D. Ligase
E. Isomerase
8. A qualitative composition of product's molecule is completely identical to substrate's one, but the
structure is different. Name the enzyme class:
A. Oxidoreductase
B. Hydrolase
C. Lyase
D. Ligase
E. Isomerase
9. ATP molecules may be used for Transferases and Ligases function. Point out the ATP using
signs 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's bond
D. ATP is used for the new bond formation during the interaction of two substrates
E. ATP is used for a substrate decarboxylation8.
10. The active centre of the enzyme contains amino acid residues of Asp. The substrate for this
enzyme is organic alcohol. Point out the type of bond that may be formed between this
substrate molecule and active centre of this enzyme:
A. Glycosidic bond
B. Hydrogen bond
C. Peptide bond
D. Ester bond
E. Disulfide bond
LESSON 5
THEME: A MECHANISM OF ENZYME CATALYSIS. ENZYME KINETICS. A REGULATION OF
ENZYME ACTIVITY.
1.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
2. There are some factors influencing enzyme activity. Point out one of them resulting in complete
loss of enzymatic activity:
A. Vitamin H
B. Сarbon dioxide
C. T = 1000 C
D. P =101325 Pa
E. Sodium chloride solution
3. There are some characteristic sites in the enzyme structure. Choose the most important site for
enzyme`s function:
A. Allosteric centre
B. Active centre
C. Cofactor
D. Apoenzyme
E. Catalytic site
4. The mechanism of enzyme's action can be described with the equation. Find the correct
variant of the equation for an irreversible enzymatic reaction:
5. Choose the factor that changes the enzyme conformation:
A. Suicide inhibitor
B. Environmental pH
C. Environmental temperature
D. Allosteric inhibitor
E. Metabolite
6. Point out the way of proenzyme transformation to the active enzyme:
A. Limited proteolysis
B. Dehydratation
C. Decarboxylation
D. Inhibitor’s action
E. Non-protein part dissociation from enzyme
7.Competitive inhibitor always interacts with enzyme active centre. Explain the reason:
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 centre
8. Covalent modification of inactive form of enzyme is catalyzed by special enzyme in a cell.
Name it:
A. Esterase
B. Peptidase
C. Proteinkinase
D. Hydroxylase
E. Oxygenase
9. Find out the irreversible type of enzyme inhibition:
A. Competitive
B. Noncompetitive
C. Uncompetitive
D. Allosteric
E. Suicide
10. Find out the mathematic significance of Michaelis constant (Km):
A. It is a time for complete degradation of a substrate
B. It is a hulf of a substrate concentration for obtaining of Vmax
C. It is a substrate concentration for obtaining of 1/2 Vmax
D. It is a constant for ES-complex dissociation
E. It is a product concentration formed after enzymatic reaction
LESSON 6
THEME: DETERMINATION OF ENZYME ACTIVITY. ISOZYMES. MULTIENZYME SYSTEMS IN
A CELL. ENZYMES IN MEDICINE.
1. 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 native protein structure
B. Different level of structural organization in native molecule
C. Different by the type of coenzyme in native molecule
D. Different by the quantity of subunits
E. Different by the combination of subunits, forming a native molecule
2. Point out the activator, used for the determination of urine's amylase activity under Volhemut's
method:
A. CuSO4
B. NaCl
C. H3PO4
D. ATP
E. Ca2+
3. 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
4. Point out the signs of multienzyme systems (MS):
A. The MS enzymes are united only by their intracellular localization
B. The MS enzymes form a single structural-functional complex
C. The MS enzymes form several different metabolic products at once
D. The MS enzymes use one and the same cofactor
E. The MS enzymes use one and the same substrate for getting different metabolic products
5.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. The Unit of an enzyme`s activity
6. Find out the substrate used for amylase activity determination in the urine of patient:
A. Glucose
B. Pyruvate
C. Maltose
D. Glycogen
E. Starch
7. 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
8.Pyruvate dehydrogenase complex is multienzyme system because it contains:
A. Two enzymes and one coenzyme
B. Two enzymes and five coenzymes
C. Three enzymes and three coenzymes
D. Three enzymes and five coenzymes
E. Five enzymes and five coenzymes
9.There is the treatment of patients with achlorhydria (the absence of free hydrochloric acid in
the gustric juice of patient) by enzyme as a drug. Name it:
A. Rennin
B. Pyruvate
C. Pepsin
D. Trypsin
E. Chymotrypsin
10.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
LESSON 7
THEME: COMMON WAYS OF CATABOLISM. ENERGY EXCHANGE. KREBS CYCLE. TISSUE
RESPIRATION.
1. Point out the substrate of Krebs Cycle (KC) that can be the product of the last reaction of KC:
A. Oxaloacetate
B. Citrate
C. a-ketoglutarate
D. Malate
E. Succinate
2. Nucleoside triphosphate is formed in Krebs Cycle. Point out its abbreviation:
A. ATP
B. CTP
C. GTP
D. UTP
E. TTP
3. Only one of Krebs Cycle dehydrogenases has the non-protein part FAD. Name it:
A. Isocitrate dehydrogenase
B. a-Ketoglutarate dehydrogenase
C. Malate dehydrogenase
D. Succinate dehydrogenase
E. Pyruvate dehydrogenase
4. One of Krebs Cycle dehydrogenases is a multienzyme complex. Point out it:
A. Isocitrate dehydrogenase
B. a-Ketoglutarate dehydrogenase
C. Malate dehydrogenase
D. Succinate dehydrogenase
E. Pyruvate dehydrogenase
5. Vitamin B1 (coenzyme TPP) is necessary for only one dehydrogenase function in Krebs Cycle.
Point out it:
A. Malate dehydrogenase
B. a-Ketoglutarate dehydrogenase
C. Isocitrate dehydrogenase
D. Succinate dehydrogenase
E. Lactate dehydrogenase
6. HADH is formed as a product in Krebs Cycle. Point out the mole quantity of HADH per 1 mole
of acetyl~SCoA:
A. 1
B. 2
C. 3
D. 4
E. 1, 5
7. KC is one of stages in catabolic ways. Point the number of stage, which is related to Krebs Cycle:
A. 1
B. 2
C. 3
D. 4
E. 5
8. Krebs Cycle is an amphiobolic way. Choose the explanation of this sentence:
A. It forms CO2 and H2O
B. It forms HADH
C. Substrates of KC can be used in anabolic ways
D. 1 mole of ATP will be formed in one cycle
E. The process is in mitochondrion
9. Two reactions of Krebs Cycle (KC) are named as oxidative decarboxylation. Point out the
enzyme of this type of reaction in KC:
A. Citrate synthase
B. cis-Aconitate hydratase
C. Isocitrate dehydrogenase
D. Succinate dehydrogenase
E. Succinyl~SCoA synthase
10. Point the stage with maximum ATP energy formation for glycose aerobic destruction up to CO2
and H2O:
A. Glycolysis up to pyruvate
B. Oxidative decarboxylation of pyruvate
C. Krebs Cycle
D. Glycolysis to lactate
E. None of these processes
LESSON 8
THEME: ENERGY EXCHANGE. OXIDATIVE PHOSPHORYLATION. BIOLOGICAL
MEMBRANES: STRUCTURE AND PROPERTIES (seminar)
1. The patient suffering from insomnia (sleeplessness) was prescribed barbiturate sleeping pills.
Name the enzyme of mitochondria that is inhibited by this drug:
А. Cytochrome oxidase
В. NADH-dehydrogenase
С. Succinate dehydrogenase
D. Isocitrate dehydrogenase
Е. a - ketoglutarate dehydrogenase
2. The antibiotic oligomycin has been recently used in tuberculosis treatment. Point out the process
in tuberculous bacillus thatis inhibited by this drug:
А. Oxidative phosphorylation
В. Translation
С. Anaerobic glycolysis
D.The active transport of substances across membranes
Е. Phagocytosis
3. High concentrations of T3, T4 in the patient suffering from Basedow disease are followed by the
infringement in the tissue energy supply. Point the right reason of this state:
А. T3, T4 intensify the adsorbtion of Ca2+ in the thin intestine
В. T3, T4 play the role of uncouplers of oxidation and phosphorylation
С. T3, T4 inhibit the dehydrogenases of Krebs Cycle
D. T3, T4 activate the lipolysis
Е. T3, T4 reduce the respiratory control up to zero
4. The increasing of NH3 in the blood plasma leads to the tissue respiration blockade. How will the
respiratory control change in the blood cells in this case?
А. ATP/ADP will rise
В. ATP/ADP will reduce
С. ATP/ADP will not change
D. ATP/ADP = 0
E. ATP/ADP becomes negative
5. The important catabolic processes are located in the mitochondrial matrix. Find out the catabolic
process that isn't located in the mitochondria:
А. Krebs Cycle
В. Oxidation of fatty acids to acetyl~SCoA
С. Oxidative decarboxylation of pyruvate
D. Glycolysis
Е. The formation of oxaloacetate from pyruvate
6. The tissue respiration is inhibited after coal gas poisoning. Point the respiratory chain enzyme
whose activity abruptly reduces in this condition:
А. Succinate dehydrogenase
В. NADH - dehydrogenase
С. Cytochrome b1
D. Cytochrome c
Е. Cytochrome aa3
7. Rotenone (the inhibitor of the first complex of the respiratory 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 the malate that is oxidized:
А. <1
В. <2
С. <3
D. <4
Е. 0
8. Name the Krebs Cycle enzyme whose activity is increasing while the value of the respiratory
control (ATP/ADP) is reducing:
А. Isocitrate dehydrogenase
В. Malate dehydrogenase
С. Pyruvate dehydrogenase
D. Succinate dehydrogenase
Е. a - ketoglutarate dehydrogenase
9. The increase of one substrate concentration occurs in the mitochondrial matrix during the
inhibition of Citrate synthase in Krebs Cycle. Find out this substrate:
А. Pyruvate
В. Acetyl ~ SCoA
С. a-ketoglutarate
D. Malate
Е. Succinate
10. The electrochemical potential (DmH+) formation occurs on the inner membrane of
mitochondria during the active work of the respiratory chain. Point out the substance that can
reduce the (D mH+) value:
А. Succinate
В. Malonic acid
С. 2,4-dinitrophenol
D. Citric acid
Е. Glucose
LESSON 10
THEME: CHEMISTRY OF CARBOHYDRATES. CARBOHYDRATES DIGESTION IN GIT.
ANAEROBIC GLYCOLYSIS.
1. What substance is a carbohydrate:
A. Arabinose
B. Amylase
C. Glutatione
D. Hexokinase
E. Glycocholic acid
2. Determine, what is the chemical structure of monosaccharides:
A. Glycerol ethers
B. Glucose amino derivatives
C. Aldehydes or ketones of polyatomic alcohols
D. Polypeptides
E. Derivatives of phosphatidic acid
3. Indicate the main signs for monosaccharides classification "They are called due to:
A. The quantity of oxygen atoms
B. The quantity of carbon atoms
C. The quantity of hydrogen atoms
D. An elementary composition
E. Physico-chemical properties
4. Restorative properties of monosaccharides are caused by:
A. Carboxylic group
B. Methylic group
C. Amino group
D. Aldehydic group
E. Sulfhydrilic group
5. Choose the disaccharide:
A. Ribose
B. Glycogen
C. Lactose
D. Galactose
E. Raphinose
6. Point out the type of bonds between glucose-monomers in starch:
7. Choose the end product of anaerobic glycolysis:
A. Pyruvate
B. Acetyl-SCoA
C. Lactate
D. CO2, H2O
E. Oxaloacetate
8. What enzyme catalyzes the glucose-6-phosphate formation from glucose in the liver:
A. Hexokinase
B. Glucokinase
C. Pyruvate kinase
D. Glucose-6-phosphatase
E. Phosphoglucomutase
9. What enzyme takes part in the gastric digestion of carbohydrates:
A. Oligo-1,6-glycosidase
B. Amylo-1,6-glycosidase
C. Salivary amylase
D. There's no any enzyme for carbohydrates digestion in stomach
E. Sucrase
10. Choose the qualitative reaction to disaccharides:
A. Trommer's reaction
B. Reaction with iodine
C. Reaction with naphtole
D. Reaction with diphenylamine
E. Barfed's reaction
LESSON 11
THEME: AEROBIC OXIDATION OF CARBOHYDRATES.
PENTOSE-PHOSPHATE CYCLE
1. Choose the enzyme for the reaction of glucose transformation with ATP use:
A. Glucokinase
B. Phosphofructokinase
C. Glucose-6-phosphatase
D. Aldolase
E. Citrate synthetase
2. Point out the vitamin that does not take part in aerobic oxidation of carbohydrates.
A. Thiamine
B. Nicotinamide
C. Lipoic acid
D. Folic acid
E. Pantothenic acid
3. Point out the biological role of Pentose Phosphate Cycle:
A. HADPH and ribose-5-phosphate formation
B. Acetyl-SCоA formation
C. ATP synthesis
D. Deoxyribose formation
E. Fructose formation
4. Choose a compound that isn’t formed at oxidative decarboxylation of pyruvate:
A. Acetyl-SCоA
B. СО2
C. HADH
D. Glycerol phosphate
E. FADH2
5. Point out the location of oxidative decarboxylation of pyruvate in a cell:
A. Cytoplasm
B. Mitochondria
C. Lysosome
D. Endoplasmic reticulum
E. Nucleus
6. Choose the terminal products of aerobic glucose oxidation:
A. Lactate and ATP
B. СО2, Н2О and ATP
C. Acetyl-SCоA and ATP
D. Pyruvate and ATP
E. Citric acid and ATP
7. Point out the energy effect of aerobic glucose oxidation up to the pyruvate:
A. 2 ATP
B. 3 ATP
C. 8 ATP
D. 30 ATP
E. 24 ATP
8. Name the last stage of aerobic glucose oxidation:
A. Oxidative decarboxylation of piruvate
B. Krebs Cycle
C. Pyruvate formation
D. a-Ketoglutarate formation
E. Acetyl-SCоA formation
9. Point out the energy effect of complete glucose oxidation in aerobic condition (glycerol
phosphate shuttle mechanism is used):
A. 36 ATP
B. 38 ATP
C. 2 ATP
D. 3 ATP
E. 12 ATP
10. Name the substance that is used for electrons transport from cytoplasmic HADH to the matrix
of mitochondria:
A. Aspartate
B. a-ketoglutarate
C. Glutamate
D. Glycerate-3-phosphate
E. Malate
LESSON 12
THEME: GLUCONEOGENESIS. GLYCOGEN METABOLISM IN HUMANS. CARBOHYDRATES`
METABOLISM REGULATION.
1. Choose the correct definition of term "gluconeogenesis":
A. Glycogen synthesis from glucose
B. Glucose formation from glycogen
C. Glucose synthesis from non-carbohydrate compounds
D. Glycogen synthesis from the metabolic intermediate products
E. Glucose synthesis from other monosaccharides
2. What hormone decreases the glucose concentration in the blood, if its value is more than 6,8
mM/lit:
A. Thyroxin
B. Testosterone
C. Glucagon
D. Adrenalin
E. Insulin
3. What substance is formed in gluconeogenesis at pyruvate carboxylation?
A. Phosphoenolpyruvate
B. Malate
C. Oxaloacetate
D. Dioxyacetonphosphate
E. Succinate
4.Continue, please, the phrase:”Glycogenolysis in the liver is used for...”:
A. The decrease of glucose level in the blood
B. The increase of glucose level in the blood
C. Glucose-6-phosphate formation, only
D. The change of blood pH
E. The lactate formation
5. Choose the substance that can be the substrate for gluconeogenesis:
A. Glycogen
B. Glucose
C. Pyruvate
D. Fructose
E. Galactose
6. Point out, what enzyme`s absence is the cause of Gierke's disease:
A. a - 1,4 -glycosidase
B. Amylo- 1,6 -glycosidase
C. Glycogen-branching enzyme
D. Glucose-6-phosphatase
E. Glycogen phosphorylase
7. Point out the process that is activated in the liver first of all during essential hyperglycemia in
patient:
A. Gluconeogenesis
B. Glycogenolysis
C. Glycogen synthesis
D. Pentose Phosphate Cycle
Е. Glucoseaminoglycans synthesis
8. How glucocorticoides influence the carbohydrates exchange?
A. Stimulate the glycolysis from glucose
B. Stimulate the gluconeogenesis
C. Stimulate the starch hydrolysis in the small intestine
D. Inhibit the glycogen phosphorolysis
Е. Stimulate the glycogenesis
9. Point out the key enzyme of glycogen degradation in the liver:
А. Fructose-1,6-diphosphatase
B. Glycogen Phosphorylase
C. Glyceraldehyde-3-phosphatase
D. Glucose -6-phosphatase
E. Glucose oxidase
10. How does adrenalin influence the glucose level in the blood?
A. Increases, stimulating the glycogen destruction
B. Decreases, stimulating the gluconeogenesis
C. Does not influence
D. Decreases, inhibiting the glycogen synthesis
Е. Decreases, inhibiting the glycolysis
LESSON 13
THEME: LIPIDS: GENERAL CHARACTERISTIC, CLASSIFICATION, BIOLOGICAL
ROLE. LIPID INTESTINAL DIGESTION AND ABSORPTION. LIPIDS' TRANSPORT IN
THE BLOOD. LIPOPROTEINS. TRIACYLGLYCEROLS` METABOLISM.
1.Point out the saturated fatty acid:
A. Palmitic
B. Linolenic
C. Oleinic
D. Linolic
E. Arachidonic
2. Lipids are natural organic compounds that are:
A. Good soluble in water
B. Insoluble in organic solvents
C. Insoluble in benzene
D. Soluble in organic solvents
E. Soluble in buffer solutions
3. Point out the place of lipids' products' absorption in gastrointestinal tract:
A. Duodenum
B. Small intestine
C. Stomach
D. Esophagus
E. Bottom parts of intestine
4. Point out the end product of lipids' digestionthat is absorbed more intensively than others:
A. Bile acids
B. Mineral acids
C. Glycine
D. Monoglyceride
E. Triacylglycerols
5. Find out the enzyme of tissue lipolysis that is regulated by hormones :
A. Triacylglycerol lipase
B. Diacylglycerol lipase
C. Monoacylglycerol lipase
D. Lecitin cholesterolacyl transferase
E. Lipoprotein lipase
6. Point out the most aterogenic lipoprotein of the blood plasma:
A. HDL
B. LDL
C. IDL
D. CM
E. a-LP
7. Point out the biological role that isn't suitable for cholesterol:
A. Membranes' structure component
B. Enters into phospholipids' structure as residue
C. Substrate for steroids' hormones synthesis
D. Substrate for 1,25-dioxycholecalciferol synthesis
E. Substrate for the bile acids formation
8. Choose the separation method for lipoproteins of the blood plasm:
A. Radio immunal method
B. Extraction
C. Electrophoresis
D. Salting-out
E. Photometric method
9. The bile acids participate in:
A. The activation of trypsin
B. The lipids' emulgation
C. The cholesterol synthesis
D. The ketone bodies' synthesis
E. Protein transport activation
10. Point out the lipoprotein that keeps the biggest amount of cholesterol ester:
A. HDL
B. LDL
C. IDL
D. CM
E. VLDL
LESSON 14
THEME: LIPID METABOLISM: BIOSYNTHESIS AND DEGRADATION OF HIGH FATTY
ACIDS. GLYCEROPHOSPHOLIPIDS` METABOLIC PATHWAYS.
1. Choose the enzyme participating in Н3РО4 elimination from glycerol residue in phosphatidic
acid:
A. Phospholipase А1
B. Phospholipase D
C. Phospholipase C
D. Phospholipase А2
E. Phosphatase
2. Point out the enzyme used for lysophospholipid formation during lipolysis of
glycerophospholipid:
A. Diglyceride lipase
B. Monoglyceride lipase
C. Triglyceride lipase
D. Phospholipase A2
E. Phospholipase D
3. Point out the end product of b-oxidation of HFA (Higher Fatty Acids) with odd number of carbon
atoms:
A. Butiryl ~ SCoA
B. Malonyl ~ SCoA
C. Succynil ~ SCoA
D. Acetoacetyl ~ SCoA
E. Propionyl ~ SCoA
4. Point out the cellular location of saturated HFA synthesis:
A. Nucleus
B. Plasmolemma
C. Cytoplasma
D. Mitochondrions
E. Endoplasmic reticulum
5. Choose the allosteric activator of acetyl-CoA-carboxylase (the key enzyme of HFA synthesis) :
A. Malate
B. Oxaloacetate
C. Citrate
D. Succinate
E. Fumarate
6. Point out the biological role of carnitine in cells:
A. Antioxidant
B. Allosteric activator of enzymes
C. Transporter of acyl ~ SCoA across the mitochondria membranes
D. The component of respiratory chain
E. The enzyme inhibitor
7. Point out the substrate for acyl-CoA-dehydrogenase (b-oxidation of HFA):
A. Acetyl ~ SCoA
B. Enoyl ~ SCoA
C. Butiryl ~ SCoA
D. b-hydroxyacyl ~ SCoA
E. b-ketoacyl ~ SCoA
8. Choose the bodies and tissues where lipogenesis occurs most intensively:
A. Muscle
B. Brain
C. Liver
D. Kidneys
E. Myocardium
9.Point out, how fatty acids are activated in catabolic process:
A.Are phosphorylated by ATP
B.Don't change the structure
C.Are converted to acyl~ SCoA due to АТP energy
D. Are united with HS-CoA without any energy
E. Interact with carnitine
10.Point out the HFA that is the most presumable energy source for a cell:
A. Palmitic acid
B. Stearic acid
C. Oleic acid
D. Kidneys
E. Myocardium
LESSON 15
THEME: METABOLISM OF CHOLESTEROL, KETONE BODIES IN HUMANS.
1.Point out the metabolite, concerning to ketone bodies:
A. Acetyl ~ SCoA
B. b- hydroxybytyric acid
C. Butyric acid
D. Palmitoleic acid
E. Malonyl ~ SCoA
2.Point out the process where acetone is formed as end- product:
A. b-Oxidation of HFA
B. Decarboxylation of acetoacetic acid
C. Condensation of two acetyl-CoA molecules
D. Synthesis of HFA
E. Decarboxylation of b-hydroxybytyric acid
3. Point out the key enzyme of cholesterol synthesis:
A. Acetyl ~ SCoA carboxylase
B. b- hydroxybytyryl dehydrogenase
C. b- hydroxy-b-methylglutaryl-CoA reductase
D. Palmitate synthetase
E. Malonyl ~ SCoA-ACP transferase
4. Point out the drug used for the decrease of cholesterol level in the blood of patients - allosteric
inhibitor for key enzyme of cholesterol synthesis:
A. Aspirin
B. Lovastatin
C. Barbiturate
D. Indomethacin
E. Antimicin A
5.Point out the substance that decreases the rate of cholesterol synthesis:
A. Adrenalin
B. Thyroxin
C. Cholesterol
D. Phosphate
E. Glucose
6. Find out the coenzyme used in some reactions for ketone bodies synthesis:
A. FADH2
B. NAD
C. Pyridoxal phosphate
D. NADPH
E. Biotin
7. Find out the reason for stimulation of ketone bodies synthesis in the liver:
A. Hyperstimulation of lipolysis in the adipose tissue
B. Hypoglycemia state in patient
C. Hemolytic anemia in patient
D. The high level of insulin in the blood
E. The genetic defect of glucose-6-phosphatase
8. Find out the ketone body that is determined in the breathed out air of patient with acute diabetes
mellitus:
A. Acetoacetic acid
B. b- hydroxybytyric acid
C. Acetone
D. Acetic acid
E. Butiric acid
9. Find out the enzyme system that is used for bile acids formation from cholesterol:
A. Acetyl ~ SCoA carboxylase
B. b- hydroxybytyryl dehydrogenase
C. Acetoacetyl-CoA reductase
D. Monooxygenase cytochrome P450 -linked system
E. Malonyl ~ SCoA-ACP transferase
10. Find out the vitamin`s derivative that is synthesized from cholesterol in humans:
A. Progesterone
B. 1,25-dihydroxy cholecalciferrol
C. Estradiol
D. Cholesterol ester
E. Testosterone
LESSON 16
THEME: HORMONAL REGULATION OF CARBOHYDRATES` AND LIPIDS` METABOLISM.
PATHOLOGIES OF CARBOHYDRATES`` AND LIPIDS` METABOLISM.
1. How does adrenalin influence the activity of triglyceride lipase:
A. Doesn't influence the lipase activity
B. Activates lipase directly
C. Activates protein kinase (thanks to cAMP), which phosphorylates the lipase
D. Inhibits lipase due to cAMP
E. Inhibits lipase directly
2. Higher secretion of somatotropin leads to:
A. The stimulation of lipolysis
B. The hypophyseal obesity
C. The decrease HFA quantity in blood plasma
D. The inhibition of lipolysis
E. The activation of fats synthesis
3. Vitamin F deficiency causes the decrease of some hormones formation in tissues. Find out
them:
A. Catecholamines
B. Prostaglandins
C. Kinins
D. Glucocorticoids
E. Mineralcorticoids
4.Choose the substance, whose activity is increased inthe blood serum of patient with
atherosclerosis of blood vessels:
A. Carnitine
B. Albumins
C. High fatty acids
D. Cholesterol
E. Hemoglobin
5. Point the adrenalin effect on carbohydrates` metabolism in the liver:
A. Stimulates lipolysis
B. Stimulates glycogenolysis
C. Inhibits glycolysis
D. Inhibits Krebs Cycle
E. Stimulates Pentose Phosphate Cycle
6. Point out the pathological state that is accompanied with the increase of glucose level in
the blood:
A. Acute pancreatitis
B. Nephritis
C. Tyrosinemia
D. Atherosclerosis
E. Viral hepatitis
7.Point out the process that is the supplier of NADPH for fatty acids` synthesis:
A. Gluconeogenesis
B. Pentose Phosphate Cycle
C. b-Oxidation of fatty acids
D. Glycolysis
E. Glycogenolysis
8.Point out the normal value of atherogenic coefficient in adults:
A. >2,0
B. Ј3,0
C. >3,5
D. >4,0
E. <1,5
9.Point out the hormone that inhibits the duration of lipolysis :
A. Somatotropic hormone
B. Prostaglandin E2
C. Adrenalin
D. Glucagon
E. ACTH
10.Find out the key metabolite formed in glucose oxidation and used for lipogenesis:
A. Phospholipid
B. Acyl-CoA
C. Acetyl-CoA
D. Peptide
E. Ammonia
LESSON 19
THEME: DIGESTION OF PROTEINS IN THE GASTROI-NSTESTINAL TRACT. CONVERSION
OF AMINO ACIDS UNDER THE INFLUENCE OF INTESTINAL MICROFLORA
AND NEUTRALIZATION OF TOXIC PRODUCTS IN THE LIVER.
1. Point out the class of enzymes that catalyze the digestion of proteins in gastro-intestinal tract:
A. Transferases
B. Lyases
C. Hydrolases
D. Oxidoreductases
E. Ligases
2. Point out bonds, which are destructed by proteolytic enzymes:
A. Phosphodiester
B. Ester
C. N-glycoside
D. Peptide
E. Disulfide
3. Point out the group of peptidases which trypsin is belong to
A. Aminopeptidase
B. Exopeptidase
C. Endopeptidase
D. Dipeptidase
E. Carboxypeptidase
4. Point out the value of pH, which is optimal for the activity of pepsin:
A. 6,8 - 7,2
B. 3,5 - 4,8
C. 7,2 - 8,5
D. 1,5 - 2,5
E. 8,5 - 10,0
5. Point out the couple of amino acids participating in the formation of peptide bond that is cleaved
by trypsin:
A. Arginine, lysine
B. Leucine, valine
C. Glycine, Glutamine
D. Alanine, valine
E. Isoleucine, alanine
6. Point out the amino acids whose peptide bonds are hydrolyzed by pepsin and chymotrypsin:
A. Diamino acids
B. Aromatic amino acids
C. Dicarboxylic acids
D. Alcoholic acids
E. Sulfur-containing amino acids
7. Point out the component of pancreatic juice that neutralizes the chymus pH in the duodenum:
A. Lipase
B. Glucagon
C. Trypsin
D. Sodium hydrocarbonate
E. Insulin
8. Point out the endopeptidase that is produced by pancreas and is activated by trypsin:
A. Proelastase
B. Renin
C. Pepsinogen
D. Gastricsin
E. a-Amylase
9. Point out the enzymes' class, participating in limited proteolysis of endopeptidases’ precursors:
A. Oxydoreductases
B. Lyases
C. Hydrolases
D. Isomerases
E. Transferases
10. Point out the activator of secretin production in duodenum:
A. Hydrochloric acid
B. Pepsin
C. Gastricsin
D. Trypsin
E. Chymotrypsin
LESSON 20
THEME: COMMON WAYS OF AMINO ACIDS' CATABOLISM.
1. Point out the way of of Amino Acids` transformation that is not the common catabolic pathway:
A. Transamination
B. Transdeamination
C. a-Decarboxylation
D. Oxidative deamination
E. Hydroxylation
2. Point out the liver enzyme, which takes part in the transdeamination of Amino Acids:
A. a-Ketoglutarate dehydrogenase
B. Glutamate dehydrogenase
C. Glutamate decarboxylase
D. L-Alanine oxidase
E. Tryptophan hydroxylase
3. Point out the enzyme, whose activity is determined in the blood plasma during the unicteric
period of viral hepatitis:
A. Phenylalanine hydroxylase
B. Creatine phosphokinase
C. Glutamate dehydrogenase
D. Alanine transaminase
E. Ornithinecarbomoylphoshate transferase
4. Choose the enzyme of the blood plasma, whose activity increases in ten or more times for 3-4
hours after myocardium infarction:
A. Alanine transaminase
B. Aspartate transaminase
C. Alcaline phoshatase
D. Arginase
E. Leucine aminopeptidase
5. Point out the cofactor, which is used by D-Amino acid oxidase in oxidative deamination:
A. NADP
B. NAD
C. FAD
D. FMN
E. TPP
6. Two biogenic amines are formed during the metabolism of Tryptophan. Point out one of them:
A. Thiamine
B. Serotonine
C. Adrenalin
D. Dopamine
E. Histamine
7. Choose the enzyme, whose genetic defect results in the GABA level`s decrease in the brain
(GABA - g-Amino Butyric Acid):
A. Tryptophan decarboxylase
B. Phenylalanine hydroxylase
C. Histidine decarboxylase
D. Alanine hydroxylase
E. Glutamate decarboxylase
8. Point out the vitamin, whose hypovitaminosis causes the violations in the transamination and
decarboxylation of Amino Acids:
A. Vitamin C
B. Vitamin B1
C. Vitamin B2
D. Vitamin B9
E. Vitamin B6
9. Point out the enzyme system that is used for serotonine synthesis from tryptophan:
A. Glutamate dehydrogenase
B. Urease
C. Monooxygenase linked cyt P450
D. Cholesterol esterase
E.a- Decarboxylase
10. Point out the enzyme of the brain catalyzing the reversible oxidative deamination:
A. Glutamate dehydrogenase
B. Alanine transaminase
C. Monoamino oxidase
D. Aspartate transaminase
E. Arginase
LESSON 21
THEME: AMMONIA DETOXYCATION WAYS. METABOLISM OF SOME AMINO ACIDS.
1. Point out the index of the blood plasma, using for the estimation of liver's parenchyma damage:
A. Glucose
B. Urea
C. Free Amino Acids
D. Cholesterol ester
E. Ca2+
2.Choose the enzyme used for tyrosine formation from phenylalanine:
A. Phenylalanine 4-monooxygenase
B. Phenylalanine transaminase
C. Dioxyphenylalanine decarboxylase
D. Aspartate transaminase
E. Tyrosinase
3. Point out the enzyme from Urea Cycle used for Arginine formation:
A. Ornithine transcarbamoylase
B. Arginine transaminase
C. Argininosuccinate lyase
D. Aspartate transaminase
E. Arginase
4. Point out the pathologic state that is estimated in patients with genetic defect of Phenylalanine
4-monooxygenase:
A. Glucosemia
B. Hyperuricemia
C. Aminoaciduria
D. Hypercholesterinemia
E. Dislipoproteinemia
5. Point out the coenzyme used for hydroxylases` structure in Phenylalanine and Tyrosine
conversions:
A. Tetrahydrobiopterin
B. Dihydrobiopterin
C. NADP
D. FAD
E. Biotin
6. Point out the pathology that is estimated in patients with genetic deficiency of Dihydrobiopterin
reductase:
A. Classic phenylketonuria
B. Gout
C. Phenylketonuria type II
D. Diabetes mellitus
E. Ishemic heart disease
7. Find out the main important way for ammonia utilization in the brain:
A. Conversion into Glucose
B. Urea formation
C. Amino Acid`s decarboxylation
D. Synthesis of Glutamine from a-ketoglutarate
E. Ammonia salts formation
8. Choose the type of infringement in pathology called Alkaptonuria:
A. Genetic deficiency of enzyme
B. The inhibition of amino acid formation
C. The renal deiciency
D. The damage of receptor`s synthesis
E. The viral damage of hepatocyte
9.Choose the hormone that is formed from tryptophan:
A. Epinephrin
B. Thyroxine
C. Norepinephrin
D. Melatonin
E. Histamine
10.Point out the enzyme deficiency that causes the hyperammonemia state in patient:
A. Ornithine transcarbamoylase
B. Arginine transaminase
C. Argininosuccinate lyase
D. Aspartate transaminase
E. Arginase
LESSON 22
THEME: MOLECULAR GENETICS BASES. NUCLEIC ACIDS BIOSYNTHESISES:
REPLICATION, TRANSCRIPTION AND REGULATION OF THESE PROCESSES.
(SEMINAR)
1. Choose the type of bonds formed during the processes of replication and transcription
A. Peptide
B. Hydrogen
C. N-glycoside
D. 3,,5
,- phosphodiester
E. Disulfide
2. The complimentary nature of pairs A - T; G - С is determined by:
A. The similarity of each couple's structure
B. The capability to form the hydrogen bonds between them
C. The equal concentration of A=T; G=С
D. The capability to form glycoside bonds between them
E. The capability to form covalent bonds between them
3. Choose the type of nucleic acid whose secondary structure reminds the cloverleaf in the
projection on a plane:
A. DNA
B. rRNA
C. mRNA
D. tRNA
4. Choose the type of nucleic acid whose secondary structure is called a-double helix:
A. DNA
B. rRNA
C. mRNA
D. tRNA
5. Point out the type of nucleic acid that is capable for the interaction with histones:
A. DNA
B. rRNA
C. mRNA
D. tRNA
6. Each polynucleotide chain of DNA contains sites, called cistrons. Choose the content of the
information kept in cistron:
A. The sequence of amino acid residues in one subunit of protein
B. The sequence of mononucleoside monophosphates of the initial transcript
C. The sequence of amino acid's residues in all subunits of protein
D. The sequence of mononucleoside triphosphates in tRNA
E. The sequence of mononucleoside triphosphates in rRNA
7. Choose the term of the uninformative site of the initial transcript:
A. Cistron
B. Intron
C. Exon
D. Operon
E. Structural gene
8. Point out the enzyme participating in the stabilization of the replication fork at E.coli:
A. Topoisomerase
B. Endonuclease
C. DNA-polymerase I
D. DNA-ligase
E. Restrictase
9. Point out the site of polynucleotide chain of DNA, which RNA-polymerase attaches to at the
initiation of transcription:
A. Reverse transcriptase
B. Primer
C. Gene-operator
D. Promotor
E. Gene-regulator
10. Point out the enzyme that is capable to connect Okazaki fragments after primers' restriction:
A. Topoisomerase
B. Endonuclease
C. DNA-polymerase I
D. DNA-ligase
E. Restrictase
LESSON 23
THEME: TRANSLATION: PROTEIN SYNTHESIS AND ITS REGULATION. MOLECULAR
DISEASES (SEMINAR)
1.Point out the derivative of the residue of N- terminal amino acid under the protein synthesis at E.
coli:
A. Isoleucine
B. Formyl threonine
C. Methionine
D. Formyl methionine
E. Leucine
2. Point out the enzyme that takes part in the peptide bond formation at the elongation stage:
A. Translocase
B. Peptidase
C. Peptidyltransferase
D. Aminoacyl-tRNA-synthetase
E. Hydrolase
3. Choose the component that doesn't take part in the initiation stage of protein synthesis:
A. mRNA
B. ATP
C. Amino acyl-tRNA
D. 30S subunit of the ribosome
E. 50S subunit of the ribosome
4. Point out the last stage of protein biosynthesis:
A. Activation of amino acids
B. Termination
C. Initiation of polypeptide chains
D. Post-translational modification
E. Elongation
5. Point out the authors of LAC-operon theory about protein synthesis regulation:
A. M. Ninenberg, S. Ochoa
B. F. Jakob, J. Monod
C. R. Okasaki
D. G. Watson, F. Crick
E. M. Meselson, F. Stahl
6. The degeneration of Genetic code is explained as such:
A. There are two or more triplets for one amino acid
B. Genetic Code is composed of various triplets
C. Each amino acid is coded for one triplet, only
D. "Punctuation marks" are absent in the Genetic code
E. Genetic code is a single for all biologic systems
7. Point out the function for amino acyl-tRNA-synthetase in protein synthesis:
A. It forms the peptide bond
B. It promotes the ribosome moving along the mRNA
C. It binds tRNA with amino acid residue
D. It takes part in the ribosome structure
E. It binds tRNA with the ribosome
8. Point out the quantity of ATP that is used during amino acid`s activation:
A. 1
B. 2
C. 3
D. 0
E. 4
9. Point out the maintenance of information keeping in the triplet A-U-G of mRNA:
A. Protein synthesis beginning from initial amino acid
B. Protein synthesis beginning and protein synthesis termination
C. Doesn't posses any information
D. Protein synthesis termination
E. The operation of post-translational modification of proteins
10. Point out the enzyme that takes part in amino acid`s activation at the first stage of protein
biosynthesis:
A. Peptidyltransferase
B. Translocase
C. Amino acyl-tRNA-synthetase
D. Amino peptidase
E. Transaminase
LESSON 24
THEME: METABOLISM OF NUCLEOTIDES: SYNTHESIS
DE NOVO AND CATABOLIC PATHWAYS
1. Choose the food product that contains the biggest part of nucleoproteins:
A. Boiled beef
B. Hen's egg
C. Macaroni
D. Cabbage
E. Cake
2.Point out the main product of nucleic acids` digestion that is formed in the small intestine:
A. Dinucleotide
B. Mononucleoside triphosphate
C. Nucleoside
D. Mononucleoside monophosphate
E. Amino acid
3. Choose the enzyme class that takes part in the digestion of 3,,5
,-phosphodiester bonds in nucleic
acids:
A. Transferases
B. Lyases
C. Hydrolases
D. Ligases
E. Oxidoreductases
4.Purine nucleotide catabolic pathways finish in human organism in forming of:
A. b-alanine
B. b-aminoisobutyric acid
C. Uric acid
D. Oxaloacetate
E. Pyruvate
5. Choose the intermediate metabolite of purine nucleotide degradation, used in the de novo
synthesis:
A. PRPP
B. Hypoxanthine
C. Adenylic acid
D. Phosphoribosylamine
E. Imidasole
6. Point out the amino acid used both in AMP and UMP de novo synthesis:
A. Glutamic acid
B. Aspartic acid
C. Glutamine
D. Inosinic acid
E. Alanine
7. Point out the vitamin that is actively used in the purine and pyrimidine nucleotide de novo
synthesises:
A. Pangamic acid
B. Ascorbic acid
C. Pantothenic acid
D. Folic acid
E. Linolinic acid
8. Two carbon atoms and the nitrogen one of the imidazole fragment in purine base skeleton are
got from only one amino acid in the de novo synthesis. Name it:
A. Glutamic acid
B. Aspartic acid
C. Glycine
D. Folic acid
E. Asparagine
9.The pyrimidine nucleotide synthesis can be considered to be the way of rendering of ammonium
toxic harmlessness, because:
A. Synthesis starts with the aspartic acid
B. The initial substrate (carbomoyl-phosphate) is formed from NH3, CO2 with ATP use
C. Phosphoribosyl pyrophosphate contains the NH3 molecule fragment
D. All the UMP nitrogen atoms are got from the NH3 molecules
E. The synthesis of all the pyrimidine nucleotides starts with the reaction with NH3
10. The pyrimidine nucleotide UMP degradation, in human organism, finishes by forming:
A. b-alanine
B. b-aminoisobutyric acid
C. Aspartic acid
D. Inosinic acid
E. Uric acid
LESSON 25
THEME: HEMOPROTEINS METABOLISM. HEMOGLOBIN: STRUCTURE, BIOLOGICAL
ROLE, SYNTHESIS AND DEGRADATION. JAUNDICES: REASONS AND
DIAGNOSTIC
1. Point out the normal form of hemoglobin that is represented by the higher concentration in the
blood of adults:
A. HbA1
B. HbA2
C. HbF
D. HbS
E. HbC
2. One of the hemoglobin form is dominated after the child's birth. This form retains in adults, but
in smaller concentration. Point out it:
A. HbA1
B. HbA2
C. HbF
D. HbS
E. HbC
3. Point out the derivative of hemoglobin that is produced after the CO poisoning:
A. Oxyhemoglobin
B. Carbhemoglobin
C. Methemoglobin
D. Carboxyhemoglobin
E. HbS
4. The concentration of one of hemoglobin derivatives increases in the patient's blood after the
nitrates poisoning. Choose it:
A. Oxyhemoglobin
B. Carbhemoglobin
C. Methemoglobin
D. Carboxyhemoglobin
E. HbS
5. Point out the correct description of the reason of iron deficiency anemia:
A. Inhibited heme synthesis according to d-aminolevulinate synthetase inactivation
B. Fe2+ including into the protoporphyrin IX is disturbed
C. Intensive erythrocytes hemolysis
D. The hemoglobin affinity to O2 is increased
E. The transferin concentration in blood is increased
6. Point out the cause of HbS appearing in case of sicle cell anemia:
A. Substitution of Glutamic acid for Valine in position 6 from the C-end in the b-chain
B. Substitution of Valine for Glutamic acid in position 6 from the N-end in the a-chain
C. Substitution of Glutamic acid for valine in position 6 from the N-end in the b -chain
D. Substitution of Glutamic acid for Valine in position 140 from the C-end in the b-chain
E. Substitution of Glutamic acid for Valine in position 46 from the N-end in the a-chain
7. Point out the first bile pigment that is produced in spleen after HbA cleavage:
A. Biliverdin
B. Verdoglobin
C. Bilirubin diglucuronide
D. Stercobilin
E. Mesobilirubin
8. Point out the bilirubin pigment that can be found in the urine of patients with hepatic jaundice:
A. Mesobilirubin
B. Conjugated biliribin
C. Unconjugated bilirubin
D. All the bilirubin forms
E. Urobilinogen
9. Point out the tissue enzyme that takes part in the heme cleavage:
A. Cycle oxygenase
B. Lipooxygenase
C. Heme oxygenase
D. Biliverdin reductase
E. Hydroxylase
10. Choose the form of the bile pigment that is normal urine component:
A. Urobilinogen
B. Stercobilin
C. Mesobilirubin
D. Uncohjugated bilirubin
E. Conjugated bilirubin
LESSON 27
THEME: BIOCHEMISTRY OF VITAMINS. QUALITATIVE AND QUANTITATIVE METHODS
FOR VITAMINS` DETERMINATION IN BIOLOGICAL OBJECTS
1.Choose the correct definition of vitamin:
A. Essential food proteins
B. Food factors that cannot be synthesized in hu-
man organism
C. Essential biologic amines
D. Organic compounds, containing amino group
E. Essential energetic food components
2. Point out the vitamin, which is soluble in lipids:
A. Vitamin C
B. Vitamin B1
C. Vitamin PP
D. Vitamin K
E. Vitamin H
3. Choose the vitamin, whose precursor is called as b-carotene:
A. Vitamin C
B. Vitamin D
C. Vitamin A
D. Vitamin B12
E. Vitamin P
4. Choose the vitamin, whose molecule structure is unsaturated cyclic alcohol (one hydroxide-group
only):
A. Vitamin K
B. Vitamin F
C. Vitamin B5
D. Vitamin D2
E. Vitamin H
5. Choose the vitamin, whose antivitamin is called as Dicoumarol:
A. Vitamin A
B. Vitamin B6
C. Vitamin C
D. Vitamin D
E. Vitamin K
6. Choose the vitamin, whose deficiency leads to osteomalacia at adults:
A. Vitamin C
B. Vitamin E
C. Vitamin D
D. Vitamin K
E. Vitamin PP
7. Choose the vitamin, which is a powerful natural antioxidant:
A. Retinal
B. Tocopherol
C. Ergocalciferol
D. Riboflavin
E. Pyridoxine
8. Choose the vitamin, whose oxidation results in blue fluorescing product in UV-rays:
A. Pyridoxine
B. Rutin
C. Thiamine
D. Folic acid
E. Ascorbic acid
9. Choose the vitamin that contains the isoalloxazine fragment in its structure:
A. Thiamine
B. Riboflavin
C. Pyridoxine
D. Ubiquinone
E. Naphtoquinone
10. Point out the vitamin, whose deficiency leads to pellagra:
A. Vitamin P
B. Vitamin A
C. Vitamin C
D. Vitamin B5
E. Vitamin B2
LESSON 28
THEME: BIOCHEMISTRY OF HORMONES. THE MECHANISM OF HORMONES' ACTION ON
A CELL. HORMONES OF PROTEN NATURE AND AMINO ACID
DERIVATIVES
1. Choose biologically active agents that are regulators of homeostasis and are secreted by special
glands:
A. Urea
B. Vitamins
C. Enzymes
D. Hormones
E. Heparin
2. Choose the biological action that is typical for hormones, only:
A. To regulate some processes in the target cell
B. To catalyze chemical reaction
C. To increase the rate of enzymatic reaction
D. To change the pH of the invironment
E. To change the conformation of protein
3. Choose the term of hormonal compounds that are secreted from hypothalamus:
A. Thomboxane
B. Agent
C. Releasing factor
D. Prostanoid
E. Antioxidant
4. Choose the department of CNS, where tropic hormones are secreted from:
A. Cerebral cortex
B. Hypophysis
C. Hypothalamus
D. Striate body
E. Yellow spot
5. Point out the chemical nature of hormones' receptors:
A. Nucleic acids
B. Carbohydrates
C. Proteins
D. Vitamins
E. Lipids
6. Choose the name of the secondary messenger that takes part in the transmisson of hormonal
signal:
A. Inositol triphosphate
B. g-Globulin
C. Cu2+
D. Transcortin
E. Cyclopentano perhydrophenanthrene
7. Point out the function for subunit C of adenylate cyclase complex:
A. Receptor
B. Energetic
C. Catalytic
D. Inductor
E. Transport
8. Find out the tropic hormone stimulated glucocorticoids secretion from adrenal cortex:
A. STH
B. ACTH
С. FSH
D. SIH
E. LH
9. Point out the location of insulin receptor:
A. Nuclea
B. Cytoplasma
С. Mitochondria
D. Cytoplasmic membrane
E. EPR smooth part
10. Point out the peculiarity that differs the hormone-like compounds from hormones:
A. The connection with receptor
B. The least molecular size
C. Production by tissue cells
D. The longest distance of the action
E. pH optimum exceeds 6.8
LESSON 29
TTHEME: BIOCHEMISTRY OF STEROID HORMONES AND EICOSANOIDS. A
CLASSIFICATION AND THE MECHANISM OF THEIR ACTION ON A CELL.
1.Point out the location of the receptor for steroid hormones in target cell:
A. Membrane
B. Mitochondria
C. Ribosome
D. Cytoplasm
E. Lysosome
2.Point out the tropic hormone that controlls (in a couple with FSH) the estrogen and androgen
secretion :
A. STH
B. ACTH
С. TTH
D. SIH
E. LH
3.Point out the hormone that is intermediate metabolite for testosterone anf estradiol synthesis:
A. Aldosterone
B. Cortisol
С. Progesterone
D. Androstenedione
E. 17-ketosteroid
4.Point out the most important function of androgens in muscles:
A. To stimulate lipolysis
B. To stimulate protein synthesis
C. To stimulate protein degradation
D. To inhibit lipogenesis
E. To stimulate muscular contraction
5. Point out the major hormone of luteal phase in females:
A. Progesterone
B. Cortisol
С. Aldosterone
D. Androstenedione
E. 17-ketosteroid
6. Find out the end-product of testosterone degradation in humans:
A. Progesterone
B. Cortisol
С. Aldosterone
D. Androstenedione
E. 17-ketosteroid
7. Find out the eicosanoid that stimulates agregation of platelets in the blood stream:
A. Prostaglandin E2
B. Leukotriene
C. Ceruloplasmin
D. Thromboxane A
E. Prostacyclin
8. Find out the key enzyme for all Prostanoids` formation in humans:
A. Cyclooxygenase
B. Prostaglandin synthetase
C. Transferase
D. Monoamino oxidase
E. Hemoglobin oxygenase
9. Point out the eicosanoid that can stimulate tissue lipogenesis:
A. Prostaglandin E2
B. Leukotriene
C. Ceruloplasmin
D. Thromboxane A
E. Prostacyclin
10. Point out the initial substrate for sex hormones` synthesis in humans:
A. Arachidonic acid
B. Cortisol
С. Aldosterone
D. Cholesterol
E. 17-ketosteroid
LESSON 30
THEME: BLOOD BIOCHEMISTRY
1.Point out the permissible range of the pH fluctuation in the blood:
A. 8,0-8,61
B. 7,37-7,44
C. 7,81-7,94
D. 6,2-6,84
E. 6,85-7,0
2. Point out the most probable location of the plasm proteins' synthesis:
A. Kidneys
B. Muscle tissue
C. Nervous tissue
D. Liver
E. Lungs
3. Point out the serum protein, participating in the blood oncotic pressure maintaining:
A. Globulin
B. Lipoprotein
C. Ceruloplasmin
D. Hemoglobin
E. Albumin
4. Point out the protein, which is absent in the blood serum of healthy people:
A. Cryoglobin
B. Albumin
C. Transferin
D. Haptoglobin
E. Hemoglobin
5. Point out the location of blood secretoric enzyme synthesis:
A. Kidneys
B. Myocardium
C. Liver
D. Spleen
E. Lungs
6. Point out the blood microelements:
A. Sodium
B. Copper
C. Calcium
D. Potassium
E. Magnesium
7. Point out the most powerful buffer system of the blood:
A. The bicarbonate buffer system
B. The phosphate buffer system
C. The protein buffer system
D. Hemoglobin buffer system
E. The acetate buffer system
8. Point out the non-protein nitrogenous component of the blood plasma that is in a level about 50%
of total non-protein nitrogen:
A. Uric acid
B. Creatine
C. Creatinin
D. Amino acids
E. Urea
9. Point out the major transport form of triacylglicerols from the intestine to the liver:
A. CM
B. LDL
C. VLDL
D. IDL
E. HDL
10. Point out the protease of blood that helps to solvate the fibrin clot:
A. Plasminogen
B. Lysolipase
C. Plasmin
D. Antifibrinogen
E. Tromboplastin
LESSON 31
THEME: PHYSICAL AND CHEMICAL PROPERTIES OF URINE. CHEMICAL COMPOSITION
OF URINE IN PATHOLOGICAL PROCESSES
1. Point out the substance that appears in the urine in case of alkaptonuria:
A. Fructose
B. Protein
C. Homogentisic acid
D. Glucose
E. Tryptophan
2. The diuresis in healthy adults is about:
A. 400-700 ml
B. 1000-2000 ml
C. 2000-3000 ml
D. 700-900 ml
E. 3000-4000 ml
3. Point out the pathological component of urine:
A. Hemoglobin
B. Urea
C. Uric acid
D. Kreatinine
E. Amino acids
4. Point out the normal component of urine:
A. Coniugated bilirubin
B. Glucose
C. Ketone bodies
D. Uric acid
E. Protein
5. What is the urine colour when intestinal rotting processes are intensified:
A. Brown
B. Straw-yellow
C. Red
D. Green or blue
E. Beer colour
6. Choose the urine component, whose concentration increases at consuming a lot of meat food:
A. Glucose
B. Protein
C. Uric acid
D. Ketone bodies
E. Fructose
7. The concentration of what urine component will decrease in case of viral hepatitis:
A. Ketone bodies
B. Protein
C. Urea
D. Lipids
E. Carbohydrates
8. Point out the qualitative reaction to blood pigments in urine:
A. Heller's test
B. Benzidine test
C. Lugol's test
D. Trommer's reaction
E. Rozine's reaction
9. The violation of the hormone secretion is followed by polyuria. Choose this hormone:
A. Adrenalin
B. Insulin
C. Sex hormone
D. Vasopressin
E. Oxytocin
10. Point out the qualitative reaction to the urine protein:
A. Heller's test
B. Benzidine test
C. Lugol's test
D. Trommer's reaction
E. Rozine's reaction
LESSON 32
THEME: METABOLISM OF FOREIGN COMPOUNDS (XENOBIOTICS). MICROSOMAL
OXIDATION IN CELLS (SEMINAR)
1. Point out the main place for location of microsomal oxidation in a cell:
A. Nucleus
B. Cytoplasm
C. EPR, smooth part
D. EPR, rough part
E. Lysosomes
2. Find the correct definition of the term "xenobiotic":
A. A substance that is an obligatory component of food products
B. A substance that is unnatural for humans
C. A substance that is synthesized in small quantities in humans
D. A substance that regulates metabolism in organism
E. A substance that is a terminal product of metabolism
3. Find the enzyme participating in the function of the microsomal monooxygenase chain:
A. НАДН - dehydrogenase
B. Cytochrome b
C. Cytochrome c1
D. Cytochrome c
E. Cytochrome P450
4. Point out the enzyme of monooxygenase chain as a final electron acceptor from the reduced
form of
NADPН:
A. Cytochrome b5
B. Cytochrome b
C. Cytochrome P450
D. Cytochrome c1
E. Cytochrome aa3
5. Monooxygenase and reductase chains of microsomal oxidation are necessary for:
A. Saturated HFA synthesis
B. Structure modification of endogenous substrates only
C. Structure modification of xenobiotics and endogenous substrates
D. Structure modification of xenobiotics only
E. Energy reception at the oxidation of xenobiotics
6. Point out the amino acid that is conjugative agent at the detoxication of xenobiotics in the liver:
A. Lactic acid
B. Glycine
C. Valine
D. Leucine
E. Histidine
7. Point out the liver enzyme participating in the neutralization of xenobiotics, their metabolites and
harmful endogenous products:
A. Glutamine synthetase
B. Glutamate dehydrogenase
C. Alanine amino transferase
D. Carbomoyl phosphate synthetase
E. UDP - glucoronyl transferase
8. Point out the peptide participating in the conjugation of some harmful products in the liver:
A. Glutation
B. Methionine
C. Trialanine
D. Oxytocin
E. Prolylproline
9. Benzoic acid has the formula C6H5-COOH and causes the cytotoxic effect at its accumulation in
the liver. Choose the conjugative agent for this substance:
A. Glycine
B. PАPS
C. S - adenosyl methionine
D. Glutation
E. Urea
10. Point out the enzyme located in the cytoplasm of
hepatocytes and participating in the modification of xenobiotics:
A. Glutamine synthetase
B. Alcohol dehydrogenase
C. Alanine amino transferase
D. Carbomoyl phosphate transferase
E. UDP - glucoronyl transferase
LESSON 33
THEME: BIOCHEMISTRY OF NERVOUS TISSUE (SEMINAR)
1. Simple and conjugated proteins are in the composition of nervous tissue. Point out the simple
proteins of this tissue type:
A. Albumins, globulins
B. Prolamins, glutelins
C. Phosphoproteins
D. Nucleoproteins
E. Lipoproteins
2. Point out the protein concentration in the white matter:
A. 20 %
B. 9 %
C. 50 %
D. 60 %
E. 80 %
3. There are special supportive proteins in the white matter of nervous tissue. Point out them:
A. Actins
B. Myosins
C. Troponins
D. Albumins
E. Neurosclero proteins
4. Point out the main catabolic pathway for glucose in the brain:
A. Aerobic glycolysis
B. Anaerobic glycolysis
C. Pentose Phosphate Cycle
D. Glycogenesis
E. Gluconeogenesis
5. The myelin substance is a complex of some compounds. What prevailing components are in it?
A. Protein, lipids
B. Carbohydrates, lipids
C. RNA, DNA
D. Adenine-linked nucleotides, creatine phosphate
E. Amino acids, mineral substances
6. Point out the lipids' concentration in the dense residue of the myelin substance:
A. 70 %
B. 90 %
C. 5%
D. 30%
E. 20%
7. Point out the neurotransmitter that is isolated in preganglionar neuron synapses of the
sympathetic nervous system:
A. Epinephrine
B. Dophamine
C. Acetylcholine
D. Glycine
E. Serotonine
8. Point out the main energy source substrate for the brain:
A. Glucose
B. Fatty acids
C. Phospholipids
D. Ketone bodies
E. Amino acids
9. Point out the enzyme that catalyzes the degradation of some neurotransmitters in the brain:
A. Aldolase
B. Glutamate dehydrogenase
C. Monoamino oxidase
D. Hexokinase
E. Malate dehydrogenase
10. There is the feature of the chemical composition of neuroglia: one acidic protein has very high
concentration. Name it:
A. Protein S-100
B. Myosin
C. Albumin
D. Choline esterase
E. Neurosclero protein
LESSON 34
THEME: MUSCCULAR AND CONNECTIVE TISSUES' BIOCHEMISTRY
1. The high levels of creatine phosphokinase (CPK) (MB - form) and lactate dehydrogenase LDH1
activity were revealed. Point out the most probable pathology in the patient:
A. Hepatitis
В. Myocardium infarction
С. Osteoartritis
D. Pancreatitis
Е. Cholecystitis
2. The patient with the electro trauma was admitted into the burn department. Point out the enzymes
whose activity is increased the most of all in blood plasma in this state (creatine phosphokinase -
CPK; lactate dehydrogenase - LDH):
A. MM - form CPK and LDH1
B. BB-form CPK and LDH5
C. MM - form CPK and LDH5
D. MB-form CPK and LDH1
Е. BB-form CPK and LDH5
3. The percentage correlation of creatine phosphokinase isozymes in miocardium is a constant value
in adults. Choose the right ratio of isozymes in this tissue type:
A. BB-3,5 %: МB-21,2 %: MM - 40,3 %
B. BB-40,3 %: МB-21,2 %: MM - 3,5 %
C. BB-1 %: МB-99 %: MM - 0 %
D. BB-90 %: МB-5 %: MM - 5 %
Е. BB-50 %: МB-1 %: MM - 40 %
4. It is established that there is specific system of energy supply in muscular cell. Point out this
system:
A. Renin-angiotensin-aldosteron system
B. Creatine phosphate kinase system
C. Adenylate cyclase system
D. Translation system of a cell
Е. Palmitate synthetase complex
5. There are some proteins in muscles: actin, myosin, actomyosin, tropomyosin, troponin. Point out
what a specific group of proteins they are related to:
A. Myofibrous proteins
B. Sarcoplasmatic proteins
C. Stroma proteins
D. Calcium conjugated proteins
Е. Coagulants
6. It is established that Creatine synthesis in the liver requiers three amino acids as sustrates in this
process. Point out them:
A. Ala, Ser, Glu
B. Arg, Gly, Met
C. Tre, Ile, Val
D. Phe, Trp, Val
Е. Ala, Val, Leu
7. Point out the major catabolic pathway of energy supply for muscular contraction in myocardium:
A. Aerobic oxidation of glucose
B. Resynthesis of АТP from UТP
C. Creatine kinase resynthesis of АТP
D. Oxidation of High Fatty Acids
Е. Synthesis of АТP from ADP
8. During the active work of muscles the energy supply is realized due to glycogenolysis. Point out
the end product of this process:
A. Pyruvic acid
B. Acetyl - CоА
C. Phosphoenolpyruvate
D. Lactate
Е. Oxaloacetate
9. The metabolism disturbance in a cardiac muscle in case of the ischemic heart disease is followed
by the decrease of АТP and creatine phosphate concentrations. Point out the reason of the
decreasing:
A. Glycolysis is activated in myocardium
B. Hypoxia in myocardium
C. Hypoglycemia
D. The oxidative phosphorylation is activated in
myocardium
Е. Hyperglycemia
10. Point out the major way of АТP synthesis in cardiac muscle:
A. Synthesis of ATP from GТP
B. Oxidative phosphorylation
C. Substrate phosphorylation
D. Synthesis of ATP from UТP
Е. Synthesis of ATP from 2 АDP molecules
LESSON 35
THEME: INTEGRATION OF THE METABOLISM PATH W AYS IN HUMAN ORGANISM.
COMMON PRINCIPLES OF THE METABOLISM REGULATION. (SEMINAR)
1. АТP is considered as energy source for a lot of synthesises in a cell. Point out the main
important process of its formation in humans:
A. Synthesis of ATP from GТP
B. Oxidative phosphorylation
C. Substrate phosphorylation
D. Synthesis of ATP from UТP
Е. Creatine phosphate kinase reaction
2. This metabolite is formed in catabolic pathway from glucose and then is used for some lipids`
synthesis. Name it:
A. Pyruvic acid
B. Acetyl - CоА
C. Phosphoenolpyruvate
D. Lactate
Е. Oxaloacetate
3. This metabolite is formed in Pentose Phosphate cycle and then is used for some lipids` synthesis.
Name it:
A. Malate
B. Acetyl-CоА
C. NADPH
D. NADH
Е. Ribose-5-phosphate
4. This vitamin`s deficiency causes the accumulation of free high fatty acids and the infringement
of all processes that they are involved in in the liver. Name this vitamin:
A. Rutin
B. Pantothenic acid
C. Pyruvic acid
D. Lactic acid
Е. Ascorbic acid
5. Name the process that is inhibited after lipolysis stimulation in the liver:
A. Synthesis of glycogen
B. Pentose Phosphate Cycle
C. Glycolysis
D. Transamination of amino acids
Е. b-Oxidation of high fatty acids
6. Name the process that is not stimulated by insulin in the target tissues:
A. Synthesis of glycogen
B. Oxidative decarboxylation of pyruvate
C. Glycolysis
D. Krebs cycle
Е.b-Oxidation of high fatty acids
7. Name the process that is stimulated in the liver of patient under poinsoning by some xenobiotics:
A. Glycogenesis
B. Pentose phosphate cycle
C. Glycolysis
D. Krebs cycle
E. Ketone bodies synthesis
8. Name the metabolite used for formation of all steroids in humans:
A. Pyruvic acid
B. Cholesterol
C. Aldosterone
D. High fatty acid
Е. Oxaloacetate
9. Name the process that is stimulated in the liver cell at the ratio ATP/ADP> 1:
A. Glycogenesis
B. Pentose phosphate cycle
C. Glycolysis
D. Krebs cycle
E. Oxidation of high fatty acids
10. Name the process that is stimulated in the liver by glucagon:
A. Glycogenesis
B. Glycogenolysis
C. Glycolysis
D. Krebs cycle
E. Cholesterol degradation
