Download Amino Acids and Simple Proteins

RUDN University
Medical Institute
Medical faculty
T.T.Berezov Biochemistry department
Programme
Discipline:
Biochemistry: molecular mechanisms of cancer
Biochemistry Programme is designed for students
interested in obtaining a Ph.D. in Biochemistry.
direction 06.06.01 «Biological sciences»,
profile «Biochemistry» (03.01.04)
Qualification: Researcher. Lecturer-researcher
Introduction
This research programme enables the studets to progress their understanding of
biochemistry and molecular biology to an advanced level and to contribute to the
progression of research in this specialist field.
The practical laboratory skills the students develop on this programme will be vital to
their study and transferable to research roles in industry. A structured programme of
training enables the students to enhance theirs abilities in scientific writing, critical
thinking, experimental design and quantitative research methods.
Our department offers in-depth coursework and diverse research opportunities that
focus on understanding the biochemical mechanisms of life’s critical molecular processes.
Research in our laboratories exposes our students to a variety of the latest methods for
sophisticated biochemical analysis, including mass spectrometry, microcalorimetry,
microarrays, fluorescence activated cell sorting, light scattering, and spectroscopic
methods, as well as modern methods for cell culture, protein purification, and
reconstitution of biochemical complexes and reactions.
The flexibility of our training program allows students to train in a number of exciting
research areas, and often allows students to develop highly effective interdisciplinary
collaborations, resulting in cutting edge thesis projects.
1. Goal of the discipline: to form the systematic knowledge about the molecular
mechanisms of biological system functions, to accommodate creation of the base for
the further study medical and clinical disciplines
2.
Linkages with the other subjects: The program is an interdepartmental major
between biology and chemistry that emphasizes the importance of a solid foundation
in the natural sciences, including mathematics and physics. The major focuses,
however, on disciplines within biology and chemistry, ranging from cell biology and
molecular biology to analytical chemistry and physical chemistry.
3. Course Competencies:
a) Universal competences (UC)
the capacity for critical analysis and evaluation of modern scientific achievements,
the ability to generate new ideas when solving research and practical problems,
including in interdisciplinary areas (UC-1); ability to design and realize a complex
research, (UC-2); the ability to plan and solve problems own professional and
personal development (UC-3)
b) General professional competences (GPC)
The ability to independently carry out research activities in relevant professional
field with the use of modern research methods (GPC-1); an ability for teaching at
the basic educational programs (GPC-2).
c) Professional competences (PC)
The ability to understand modern problems in biochemistry and use the
fundamental biological performance in the sphere of professional activities (PC-1);
An independent analysis of available information, the identification of the
fundamental problems, setting goals and objectives of the study; the performance
of the laboratory of biochemical research at solving specific problems for
specialization with the use of modern equipment and computing resources (PC-2);
An availability of skills formation of teaching material, lectures, willingness to
teach in higher education and the management of research projects students, the
ability to provide teaching material in verbal, written and graphic form(PC-3)
As a result of study a postgraduate students have:
To know:
physical and chemical nature of the processes occurring in living organisms at the
molecular, cellular, tissue and organ levels; structure and chemical properties of the
major classes of biologically important organic compounds; major metabolic pathways
converting carbohydrates, lipids, amino acids, purine and pyrimidine bases, the role of
cell membranes and transport systems in metabolism; Structure and function of the most
important chemical compounds (nucleic acids, natural proteins, and water-soluble
vitamins, hormones, etc.); physical and chemical methods of analysis in medicine
(titration, chromatographic, spectrophotometric);
the role of biogenic elements and their compounds in living organisms;
Chemistry of hemoglobin, its participation in gas exchange and maintaining acid-base
balance; the theoretical foundations of computer science in medical and biological
systems, the use of information and computer systems.
To be able to:
use of educational, scientific, popular scientific literature, the Internet portal for
academic and professional activities;
use of physical, chemical and biological equipment;
to make calculations based on the results of the experiment, carried out an elementary
statistical analysis of experimental data;
classify chemicals based on their structural formulas;
to predict the direction and the result of physical and chemical processes and chemical
reactions of biologically important substances;
use the IUPAC nomenclature for compiling the names of the formulas typical
representatives of biologically important substances;
differentiate in serum levels of normal values metabolites (glucose, urea, bilirubin, uric
acid, lactic acid and pyruvic et al.) of pathologically changed, read proteinogramma and
explain reasons for the differences; interpret research data.
To master:
chemical and biochemical terminology; basic technology of a research and
transformation of information, including with the use of educational resources training;
the concept of restrictions on the reliability and specificity of the most common
laboratory tests; skills of setting the preliminary diagnosis based on the results of
biochemical studies of human biological fluids.
4. Total efforts and Employments
Total efforts ___4_credits (144 hours)
№
Educational work
Hours (total)
Semester
1
1.
Employments (total)
80
including:
40
-
1.1
Lectures
1.2
Other classes
2
40
-
-
40
20
20
Practical works (PW) 40
20
20
-
-
-
-
including:
1.2.1
1.2.2
Seminars (S)
1.2.3
2.
Laboratory works (LW) In the interactive form (IF):
20
10
10
Individual employments (total)
64
32
32
144
72
72
4
2
2
Total efforts (hours)
Credits
5. Content of the discipline
5.1. Content of the items
1. Introduction. Proteins: structure, properties, functions
Biomolecules. The most important problems of current biochemistry. Methods of
investigations in biochemistry. Biochemistry and Medicine. Structure and Function of
Biomolecules.
Proteins - essential constituents of the living cells. Physical and chemical properties of
proteins. Composition and properties of amino acids and peptides. Four levels of structural
organization of proteins. The three-dimensional structure of proteins; role of domens and
the relationship of proteins structure to their biological functions. Methods of isolation and
purification ojf proteins.
2. Complex proteins, Nucleic acids, Enzymes
Classification of proteins: simple and conjugated proteins, composition and properties
of individual representatives of conjugated proteins. Nucleic acids. Physico-chemical
properties, composition, structure and biological role of DNA andRNA.
Enzymes: general properties, chemical structure, active centers, classification and
nomenclature, allosteric enzymes. The mechanisms of enzymatic catalysis. Structure and function of coenzymes, Kinetics of enzymatic reactions and methods for
determination of the enzymes activity, Inhibitors of enzymes, Isoen-zymes. Regulation of
the enzyme activity, Diagnostic enzymoiogy; enzymes as drugs.
3. Molecular mechanisms of regulation
Vitamins: distribution, biological role, classification. Social basis of vitamin deficiency
in some developing countries. Principles of vitamin therapy. Antivitamins. Composition and
properties of individual representatives of the fat-soluble and witer-soluble vitamins: A, D, E.
K, B1, B2, В6, B12, C, P, PP, H and Folic acid, Vitamin-like substances. Methods of
quantitative determination of vitamins in the body.
Hormones: hormone production in the endocrine glands. Molecular endocrinology.
Mechanisms of hormonal regulation of metabolism and role of the second messengers,
Chemical structure and properties of die main hormones.
4. Lipids: structure, properties, functions. Biological membranes
Hydrolyzable lipids. Non-hydrolyzable lipids. Biological roles. Fatty acids and fats.
Structure of phospholipids and glycolipids. Isoprenoids. Sterols. Steroid hormones. Bile
acids.
5. Energy metabolism
Catabolism and anabolism. Methods of metabolism investigations. Types of
metabolism and its regulation. Free energy of ATP hydrolysis. Biological oxidationreduction reactions, Chemistry of digestion. Social aspects of the rational nutrition
problems.
6. Carbohydrate metabolism
Carbohydrate metabolism: pathways of absorbed monosaccharaides. The pathway of
glycogen synthesis and degradation. Anaerobic metabolism: glycolysis, glycogenolysis and
gluconeogenesis. Aerobic metabolism: pentose phosphate pathway of glucose oxidation;
oxidative decarboxylation. of pyruvate, the tricarboxylic acid cycle. Biological oxidation,
The respiratory chain of electrons and protons transport, Oxidative phosphorylation. Energy
effect of anaerobic pathways of carbohydrate metabolism. Hormonal regulation of
carbohydrate metabolism. Pathology of carbohydrate metabolism,
7. Lipid metabolism
Lipid metabolism: pathways of the absorbed products lipid digestion, Mechanism of
b-oxidation of fatty acids, Biosynthesis of fatty acids, triacylglycerols, phospholipids and
cholesterol. Energy effect of lipid oxidation, Relationship between lipid metabolism and
carbohydrate metabolism. Intracellular lipids and blood serum lipids. Regulation of lipid
metabolism, Pathology of lipid metabolism.
8. Protein catabolism
Protein metabolism,' dynamic state of body proteins. Nitrogen balance. Problems of
adequate, balanced nitrogen nutrition. Proteolysis. Absorption and active transport of
ammo acids. Pathway of amino acids metabolism in the body: reactions of deamination,
decarboxylation, transamination and hydroxylation. Degradation of tissue proteins. Urea
cycle. Metabolism of nucleoproteins and chromoproteins. Biosynthesis and decomposition
of heme. Synthesis of purine and pyrimidine nucleotides;
9. Amino acid metabolism
Metabolism of individual amino acids. Regulation of protein metabolism, Pathology of
protein metabolism, Relationship of protein metabolism with metabolism of lipids and
carbohydrates.
10. Biochemistry of organs and tissues
Blood: composition and functions. Cellular elements. Blood plasma: composition. Plasma
proteins. Carrier electrophoresis. Erythrocyte metabolism. Distribution of iron. Hydrogen ion
concentration in the blood
Plasma. Buffer systems in the plasma. Blood clotting. Fibrinolysis. Blood groups: the ABO
system.
The family of connective-tissue cells. Extracellular proteins. Metabolism of the collagens.
Fibronectins. Proteoglycans.
Bone and teeth. Functions of calcium. Bone remodeling. Calcium homeostasis.
Structure of nerve cells . Signal transmission in the CNS . Neurotransmitters and
neurohormones. Resting potential and action Potential. Receptors for neurotransmitters. Energy
metabolism of the brain.
Organization of skeletal muscle. Mechanism of muscle contraction . Control of muscle
contraction. Energy metabolism in the white and red muscle fibers.
Functions of the kidneys . Urine formation . Organic components and Inorganic components
of the urine. Functions in the acid–base balance: Proton excretion and Ammonia excretion.
Electrolyte and water recycling. Renal hormones. Renin–angiotensin system.
Biochemistry: molecular mechanisms of cancer.
5.2. Items of the discipline and types of the works
№
Item
Introduction. Proteins: structure,
properties, functions
Complex proteins, Nucleic acids,
Enzymes
Molecular mechanisms of regulation
4
Practical and
laboratory works
PW/S LW
IF
4
2
4
4
-
2
6
4
4
-
2
6
4
4
-
2
6
5
Lipids: structure, properties, functions
Biological membranes
Biological oxidation
4
4
-
2
6
6
Carbohydrate metabolism
4
4
-
2
6
7
Lipid Metabolism
4
4
-
2
6
8
Protein catabolism
4
4
-
2
6
9
Amino acids metabolism
4
4
-
2
6
10
Biochemistry of organs and tissues
4
4
-
2
10
40
-
20
64
1.
2.
3
4
Lect
ures
40
Total
ISW
6
Hou
rs
144
5.3. Practical classes (seminars)
№
п/п
1
2
Item
Introduction.
Proteins: structure,
properties, functions
Complex proteins,
Nucleic acids,
Enzymes
Hours
Practical classes
Color reactions used for identification of protein
and amino acids. The protein precipitation reactions
The quantitative determination of protein. Dialysis
of protein. The paper chromatography of amino
acids.
Isolation of DNA from yeast cells
Effect of amylase on starch. Influence of
temperature on amylase activity
Determination of alkaline phosphotase activity.
4
4
3
Molecular
mechanisms of
regulation
4
Lipids: structure,
properties, functions
Biological
membranes
Biological oxidation
5
6
Carbohydrate
metabolism
7
Lipid Metabolism
8
Protein catabolism
9
Amino acids
metabolism
10
Biochemistry of
organs and tissues
Quantitative determination of vitamin C in potatoes,
and vitamin P in tea
Spectrophotometric determination of NADH and
calculation of purity of commercial preparation
Effect of hormones on glucose concentration in
blood.
The quantitative determination of lecitins in blood
serum (Blure Method). Quantitative determination
of cholesterol in blood serum
4
Determination of succinate dehydrogenase activity
in muscle. Quantitative determination of pyruvate in
urine
Specificity of amylase and sucrose action.
Quantitative determination of glucose in blood.
Construction of sugar curves.
Kinetics of lipase action
The quantitative determination of malonate
dialdehyde in blood serum.
Determination of gastric juice acidity
The quantitative determination of urea in urine
The quantitative determination of creatinine in
urine.
The quantitative determination of aspartate and
alanine aminotransferase activity in the blood
serum. Determination of phenylalanine in serum by
chromatography. Chromatography of amino acids.
Determination of bilirubin in blood serum The
quantitative determination of lactate dehydrogenase
and choline esterase in blood serum. Determination
of uric acid in urine
Normal and pathological components of urine.
Determination of amilase activity in urine
4
Total (hours)
4
4
4
4
4
4
40
6. Educational and methodical literature, programs
a) Literature
1. T.T. Berezov and B.F.Korovkiv. Biochemistry. – M., Mir Publishers. -1992. -515 p.
2. Baynes J. W.Medical Biochemistry. - Third Edition; - London: Elsevier, 2009. - 653
р.
3. Kuznetsova O.M., Berezov T.T., Chernov N.N. Laboratory Manual on Biochemistry.
Part 1. -М.: D IGITPRESS.-2014. -58 p.
4. Kuznetsova O.M., Berezov T.T., Chernov N.N. Laboratory Manual on Biochemistry.
Part 1. -М.: D IGITPRESS.-2015. -52 p.
5. Berezov T.T., Chernov N.N. Kuznetsova O.M. Collection of biochemistry tests . – M.
Изд-во «Оргсервис-2000». -2011. - 60с.
6. Principles of Biochemistry 4nd ed./ Lehninger, A.L., Nelson, D.L., Cox, M.M..Worth Publishing, 2004.
7. Principles of Medical Biochemistry 2nd ed./ Gerhard Meisenberg, William H.
Simmons. - Mosby Elsevier, 2006
b) Software
1. Operating system «Windows 8»
2. Software application package «Microsoft Office»
3. Testing programme «Mentor»
4. Computer programme Pharmtest; MyTestPro
c) data bases, information, reference and search systems:
1. Educational portal of the PFUR: http://web-local.rudn.ru/weblocal/kaf/rj/index.php?id=86
2. U.S. National Library of Medicine National Institutes of Health:
http://www.ncbi.nlm.nih.gov/pubmed/
3. Scientific electronic library: http://elibrary.ru/defaultx.asp
4. Electronic library system of the PFUR: http://lib.rudn.ru:8080/MegaPro/Web
5. IQlib http://www.iqlib.ru
6. Scientific electronic library Elibrary http://elibrary.ru
7. Google Academy - http://scholar.google.ru/
8. http://vak.ed.gov.ru/
7.
Equipment and Material support of the educational process
The Hitachi F-2700 Fluorescence Spectrophotometer; Microplate Absorbance Reader
TransBlot Turbo (Biorad); iMark (Biorad) xMark (Biorad); VIP Freezer MDF-U33V
(Sanyo - Panasonic); Double Beam Spectrophotometer U-2900
Photoelectric Colorimeters, centrifuges, thermo blocks, measuring burets, drying ovens,
analytical balances, Magnetic stirrers. Automatic pipettes with dispenser and others.
8. Methodological recommendations on discipline study organization
Medical biochemistry is biochemistry related to human health and disease. Its
applicative arm is clinical chemistry, a field that focuses on the methodology and
interpretation of chemical tests performed to support diagnosis and treatment.
The study of the discipline is organized according to credit-modular system using the
appropriate laboratory equipment, computers, multimedia installations.
9. Evaluation resources
1. Main terms and notions
1.1 Abbreviations
ACP Acyl carrier protein
ACTH Adrenocorticotropic hormone
(corticotropin)
ADH Antidiuretic hormone (adiuretin,
vasopressin)
ADP Adenosine 5-diphosphate
AIDS Acquired immunodeficiency
syndrome
ALA 5-Aminolevulinic acid
AMP Adenosine 5-monophosphate
ATP Adenosine 5-triphosphate
BPG 2,3-Bisphosphoglycerate
cAMP 3,5-Cyclic AMP
cDNA Complementary DNA
CDP Cytidine 5-diphosphate
cGMP 3,5-Cyclic GMP
CMP Cytidine 5-monophosphate
CoA Coenzyme A
CoQ Coenzyme Q (ubiquinone)
CTP Cytidine 5-triphosphate
DAG Diacylglycerol
DNA Deoxyribonucleic acid
ER Endoplasmic reticulum
FAD Flavin adenine dinucleotide
FMN Flavin mononucleotide
GABA γ-Aminobutyric acid
GDP Guanosine 5-diphosphate
Glut Glucose transporter
GMP Guanosine 5-monophosphate
GSH Reduced glutathione
GSSG Oxidized glutathione
GTP Guanosine 5-triphosphate
Hb Hemoglobin
HDL High-density lipoprotein
HIV Human immunodeficiency
virus
HMG-CoA 3-Hydroxy-3methylglutarylCoA
hsp Heat-shock protein
IDL Intermediate-density lipoprotein
IFN Interferon
Ig Immunoglobulin
IL Interleukin
InsP3(IP3) Inositol 1,4,5-trisphosphate
Km Michaelis constant
LDH Lactate dehydrogenase
LDL Low-density lipoprotein
MAP kinase Mitogen-activated protein
kinase
mRNA Messenger ribonucleic acid
NAD+ Oxidized nicotinamide adenine
dinucleotide
NADH Reduced nicotinamide adenine
dinucleotide
NADP + Oxidized nicotinamide
adenine dinucleotide phosphate
NADPH Reduced nicotinamide
adenine dinucleotide phosphate
NeuAc N-acetylneuraminic acid
PAPS Phosphoadenosine
phosphosulfate
PDH Pyruvate dehydrogenase
PEP Phosphoenolpyruvate
Pi Inorganic phosphate
PK Protein kinase
PLP Pyridoxal phosphate
PRPP 5-Phosphoribosyl 1-diphosphate
PTH Parathyroid hormone
Q OxidizedcoenzymeQ(ubiquinone)
QH2 Reduced coenzyme Q (ubiquinol)
rER Rough endoplasmic reticulum
RES Reticuloendothelial system
RNA Ribonucleic acid
ROS Reactive oxygen species
rRNA Ribosomal ribonucleic acid
SAH S-adenosyl L-homocysteine
SAM S-adenosyl L-methionine
sER Smooth endoplasmic reticulum
sn Stereospecific numbering
snRNA Small nuclear ribonucleic acid
THB Tetrahydrobiopterin
THF Tetrahydrofolate
TPP Thiamine diphosphate
TRH Thyrotropin-releasing hormone
(thyroliberin)
tRNA Transfer ribonucleic acid
TSH Thyroid-stimulating hormone
(thyrotropin)
UDP Uridine 5-diphosphate
UMP Uridine 5-monophosphate
UTP Uridine 5-triphosphate
UV Ultraviolet radiation
Vmax,V Maximal velocity(of an
enzyme)
VLDL Very-low-density lipoprotein
1.2 Terms
1. Acetyl CoA.
2. Actin.
3. Activated complex.
4. Active site.
5. Active transport.
6. Adenine.
7. Adenosine diphosphate
8. Adenosine triphosphate
9. Adenosine.
10. Adenylate cyclase.
11. Adipocyte.
12. Aerobe.
13. Afinity chromatography.
14. Alcohol.
15. Aldehyde.
16. Allosteric enzyme.
17. Amino Acid.
18. Anomers.
19. Antibody.
20. Anticodon.
21. Antigen.
22. Apoprotein
23. Asymmetric carbon.
24. ATP "Adenosine triphosphate".
25. Autoregulation.
26. B cell.
27. Beta-bend (-bend) or turn.
28. Beta-oxidation (-oxidation).
29. Beta-sheet (-sheet).
30. Bilayer.
31. Bile salts.
32. Bond energy.
33. Branchpoint.
34. Buffer.
35. cAMP.
36. Carbohydrate.
37. Carboxylic acid.
38. Carcinogen.
39. Carotenoids.
40. Catabolism.
41. Catalyst.
42. Catalytic site.
43. cDNA.
44. Cellulose.
45. Chelate.
46. Chemiosmotic coupling.
47. Chiral compound.
48. Chitin.
49. Chromatography.
50. Citric acid cycle.
51. Coactivator.
52. Coenzyme.
53. Cofactor.
54. Collagen.
55. Complementary base sequence.
56. Configuration.
57. Conformation.
58. Constitutive enzymes.
59. Cooperative binding.
60. Cytidine.
61. Cytochromes.
62. Cytokinin.
63. Cytosine.
64. De novo pathway.
65. Deamination.
66. Dehydrogenase.
67. Denaturation.
68. Dialysis.
69. Dimer.
70. Disulfide bridge.
71. DNA polymerase.
72. Deoxyribonucleic acid.
73. Domain.
74. Double helix.
75. Eicosanoid.
76. Electrophoresis.
77. Eluate.
78. Endergonic reaction.
79. Endocrine glands.
80. Endopeptidase.
81. Endoplasmic reticulum.
82. Enzyme.
83. Epimers
84. Ether.
85. Exergonic reaction.
86. Exon.
87. Exonuclease.
88. Fatty acid.
89. Feedback inhibition.
90. Fermentation.
91. Free energy.
92. Furanose.
93. Gel fitration chromatography.
94. Globular protein.
95. Gluconeogenesis.
96. Glucose.
97. Glycogen.
98. Glycogenic.
99. Glycolipid.
100. Glycolysis.
101. Glycoprotein.
102. Glycosidic bond.
103. Growth factor.
104. Guanine.
105. Guanosine.
106. Half-life.
107. Helix.
108. Heme.
109. Hemiacetal.
110. Hemoglobin.
111. Heteropolymer.
112. Hexose.
113. High-energy compound.
114. Histones.
115. Holoenzyme.
116. Homopolymer.
117. Hormone receptor.
118. Hormone.
119. Hydrogen bond.
120. Hydrolysis.
121. Hydrophilic.
122. Hydrophobic effect.
123. Hydrophobic.
124. Imine.
125. Immunoglobulin.
126. Induced fit.
127. Inducible proteins.
128. Interferon.
129. Isoelectric point or pH.
130. Isomerase.
131. Isomerization.
132. Ketogenic.
133. Ketone bodies.
134. Ketone.
135. Ketosis.
136. Kinase.
137. Krebs cycle.
138. Ligand.
139. Ligase.
140. Lipid bilayer.
141. Lyase.
142. Lysosome.
143. Membrane protein.
144. Membrane.
145. Messenger RNA (mRNA).
146. Micelle.
147.
148.
149.
150.
151.
152.
153.
154.
155.
156.
157.
158.
159.
160.
161.
162.
163.
164.
165.
166.
167.
168.
169.
170.
171.
172.
173.
174.
175.
176.
177.
178.
179.
180.
181.
182.
183.
184.
185.
186.
187.
188.
189.
190.
191.
192.
193.
194.
195.
196.
197.
198.
Michaelis constant (Km).
Mitochondrion.
Monomer.
Mutarotation.
Myosin.
Negative control.
Nitrogen fixation.
Nitrogenous base. .
Noncompetitive inhibitor.
Northern blotting.
Nuclease.
Nucleic Acid.
Nucleic acids.
Nucleophilic group.
Nucleoside.
Nucleotide.
Oligosaccharide.
Oncogene.
Optical activity.
Oxidation.
Oxidative phosphorylation.
Oxidoreductase.
Pentose phosphate pathway.
Pentose.
Peptide.
Peptidoglycan.
Permeable.
Peroxisomes.
Phenylketonuria.
Phosphate.
Phosphodiester.
Phospholipid.
Pigment.
Polar group..
Polyamine.
Polymer.
Polymerase.
Polynucleotide phosphorylase.
Polynucleotide.
Polypeptide.
Polysaccharide.
Porphyrin.
Posttranslational modification.
Primary structure.
Primer.
Proprotein.
Prostaglandin.
Prosthetic group.
Protamines.
Protein subunit.
Protein.
Proteoglycan.
199.
200.
201.
202.
203.
204.
205.
206.
207.
208.
209.
210.
211.
212.
213.
214.
215.
216.
217.
218.
219.
220.
Purine.
Pyranose.
Pyrimidine.
Pyrophosphate.
Regulatory enzyme.
Renaturation.
Ribose.
Salting out.
Salvage pathway.
Second messenger.
Secondary structure.
Semipermeable.
Southern blotting.
Splicing.
Starch.
Stereoisomers.
Steroids.
Structural domain.
Structural protein.
Substrate.
Subunit.
Sugar.
1.3.
221.
222.
223.
224.
225.
226.
227.
228.
229.
230.
231.
232.
233.
234.
235.
236.
237.
238.
239.
240.
241.
242.
TCA cycle.
Terpenes.
Tertiary structure.
Tetramer.
Thioester.
Thymidine.
Thymine.
Transamination.
Transcription.
Transfer RNA
Transferase.
Transition state.
Translation.
Transport protein.
Tricarboxylic acid cycle.
Trypsin.
Turnover number.
Ultracentrifuge.
Urea cycle.
Vitamin.
Zwitterion.
Zymogen
Guidelines for students
Guidelines for students are published in the forms of academic manuals and textbooks
1) Laboratory Manual on Biochemistry. Part 1 Kuznetsova O.M., Berezov T.T., Chernov
N.N. М.: DIGITPRESS. 2014. 58 P
2) Laboratory Manual on Biochemistry. Part 2 Kuznetsova O.M., Berezov T.T., Chernov
N.N. М.: DIGITPRESS. 2015. 51 P
3) Collection of biochemistry tests. Berezov T.T., Chernov N.N. Kuznetsova O.M. M.:
Изд-во «Оргсервис-2000». 2011, - 60 P.
1.4.
Grade System
Intermediate control (IC) includes written test (5 points) and computer test (5 points).
The number of IC is 10 in accordance with the number of topics.
Final examination is a written or computer test (100 points).
Final mark is calculated according to the relation:
IC (out of 100) + Final exam (out of 100)/ 2 =
GRADING SCALE:
Final grades will be based on the following scale:
ECTS
A
B
Traditional marks in
the Russian
Federation
5
Rating points
Marks
95 - 100
86 - 94
5+
5
C
D
E
FX
F
4
3
2
69 - 85
61 - 68
51 - 60
31 - 50
0 - 30
4
3+
3
2+
2
2. Examples of the questions for a self-examination and discussion in a class
Topic 1
1. Asparagine contains the amide group
2. Protein molecules in solution are stabilyzed by electrical charge
3. Characteristic for cyclic amino acids is xanthoprotein reaction
4. The mixture of free amino acids gives the positive ninhydrin reaction
5. Precipitation of proteins from solution is more effective in Isoelectric point
6. Serine contains a free hydroxyl group
7. Valine, leucine and isoleucine possesse the hidrophobic properties
8. Are all proteins soluble in water?
9. Are the peptides bonds spleted during thermal denaturation of protein?
10. Does the mixture of free amino acids possess the positive biuret reaction?
11. Is the ornithine a component of native protein?
12. May the methionine be considered as derivatives of butyric acid?
13. Imidasol ring contains 1 nitrogen atom
14. N-Terminal amino acid in depeptide: Histidyl-Lysine is Histidine
15. C-Terminal amino acid in thripeptide: Serylprolylglycine is Glycine
16. Albumins of blood serum carry out the transport function
17. Proline contains the imino group
18. Aspartic acid is the derivatives of succinic acid
19. Do the all peptides give the positive biuret reaction?
20. Does the colour intensity of substance in solution depend from its concentration?
Topic 2
1. Prostetic groups of nucleoproteins are represented by nucleic acids.
2. Carbohydrates could not be as prostetic group for complex proteins.
3. Phosphoric acid in phosphoproteins is joined through hydroxyl group of serine, threonine
or tyrosine.
4. The minor bases more often meet (contain) in tRNA composition.
5. Protamines and histons are the component of nucleoproteins.
6. Myoglobin belongs to chromoproteins.
7. Are there differences in chemical structure of proteins and nucleic acids?
8. May be splited the hydrogen bonds during protein denaturation?
9. Are there nucleic acids the polynucleotides?
10. Are there distinguishes in quantity by carbon atoms in molecule of ribose and
dexyribose?
11. The specificity of complex enzyme is determined by coenzyme.
12. The active site of enzyme consists from substrate binding and catalytic sector (site)
13. The enzyme activity do not depends from substrate concentration.
14. The enzymes catalyze both forward and revers reactions.
15. The velocity of enzyme reaction is always accelerated with the rise of pH medium.
16. The pepsin possesses with absolute specificity of action.
17. Is the enzyme-substrate complex always is formed during enzymatic reactions?
18. Does the velocity of enzymatic reaction depend from the enzyme concentration?
19. Does the ions of heavy metals influence on the enzyme activity?
20. May the enzymes be separated by ammonium sulfate precipitation?
Topic 3
1. Carotine is the precursor of the vitamin A.
2. Vitamin E and K are the derivatives of sterols.
3. Vicasol is soluble in water.
4. Cobalt is the component of vitamin B 12.
5. Biotin (vitamin H) takes part in assimilation of carbon dixide by enzymes.
6. Vitamin B2 is the component of flavinmononucleotide (FMN).
7. Does the vitamin K takes part in the course of blood coagulation.
8. Are the known antivitamins of B1?
9. Is the vitamin B6 a component of coenzyme A?
10. Does the folic acid take part in the synthesis of purine nucleotides?
11. Lipids are hydrophilic compounds.
12. Palmitate and oleate have equal number of carbon atoms.
13. Cholesterides are the esters of cholesterol and higher fatty acids.
14. Hexose is a component of cerebrosides.
15. Cardiolipin belongs to glycerolipids.
16. To group of the licanosoids belongs: prostaglandins, prostacyclins, tromboxancs, and
leucotrienes.
17. Hormons are able to regulate the activity of individual anzyme or enzyme systems.
18. Biological activity of hormons develops under very low of their concentration in blood.
19. Aldosteron belongs to glucocorticoids.
20. Vasopressin is the anterior pituitery hormon.
Topic 4
1.
2.
3.
4.
5.
6.
7.
The conversion of glucose into glycogen is called glycogenolysis
Glycogen is a storage material.
Glucose cannot enter the brain without insulin
Glucagon secretion stimulates glycogenolysis.
Gluconeogenesis is the conversion of glycogen to glucose
Glucagon raises blood glucose
Glyceraldehyde-3-phosphate dehydrogenase catalyzed step is the main step for energy
yield under anaerobic conditions
8. Glycerol kinase is absent in the adipose tissues
9. Phosphoglycerate kinase catalyzed step yields energy by substrate level phosphorylation
10. Diabetic ketoacidosis is a commonest complication of type 2 diabetes mellitus
11. Insulin receptor has tyrosine kinase activity
12. Acetyl-CoA is an ideal substrate for gluconeogenesis
13. Insulin promotes lipolysis by stimulating hormone sensitive lipase
14. Oral glucose tolerance test is a confirmatory test in suspected case of diabetes mellitus
15. Aconitase enzyme catalyzes the condensation of Acetyl-CoA and oxaloacetate
16. Muscle glycogen functions to store and export glucose to maintain blood glucose between
meals
17. Liver and kidney are the major gluconeogenic tissues
18. Glucose-6-phosphate dehydrogenase is an NAD+ dependent enzyme
19. Ribose cannot be synthesized in all tissues
20. The rate of TCA cycle is reduced when the cell has a high level of ATP
Topic 5
1. Lipids are splited until free fatty acids.
2. Palmitate and oleate are the unsaturated compounds.
3. Chylomicrons are the transport forms of triacylglycerols.
4.
5.
6.
7.
8.
9.
Glycerol is not a lipid.
In the presence of bile lipase action is accelerated.
The lipid acids activation is needed in energy spend.
Does the carnitine takes part in fatty acids oxidation?
May glycerol be transform into 3-phosphoglyceraldehyde in living cell?
Does the preliminary activation of fatty acids needed for the biosynthesis of neutral
lipids?
10. May the proteins be splited under lipase action?
11. In β-oxidation of fatty acids take part FAD-, and NAD-dependent dehydrogenases.
12. The complete oxidation of 1 mole of palmitate till CO2 and H2 O is accompaned with
formation of 130 molecules of ATP.
13. Linolenic acid is essential for human.
14. Mevalonic acid synthesis is needed in the presence of NADP·H2 .
15. Prostaglandins are synthesized from polyansaturated futty acids
16. Cholesterol in blood serum exist only in free state.
17. May NADP·H2 be changed or substituted by NAD·H2 in the cours of higher fatty acid
synthesis?
18. Takes the biotin part in the fatty acids synthesis?
19. Is the complete convertion of neutral lipids into carbohydrates possible in animal
organisms?
20. Are there all stages of β-oxidations of fatty acids reversible in mitochondria?
Topic 6
1.
2.
3.
4.
Proteinases, amylases and lipases belong to class of hydrolase.
Taurine is the metabolite product of cysteine.
Scatol and indol are formed in intestine from amino acid tyrosine.
Hydrochloric acid in stomach activates the pepsinogen.
5.
During deamination of amino acids in organism the biogenic amines are formed.
6.
7.

9.
Tyrosine is the essential amino acid for human.
Different coenzymes may take part in oxidative deamination of amino acid.
The transamination reactions of amino acids are irreversible.
-Ketoglutarate takes part in both transdeamination and transreamination of amino
acids.
10.
FAD is the coenzyme for aminotransferases.
11.
In the course of transamination ammonia is liberated.
12.
Is the convention of pyruvate into alanine possible in organism of human?
13.
Is the phenylalanine a precursor for serotonin?
14.
May the determination of aspartate amino transferase activity in blood serum be
used for diagnosis of heart infarction?
15.
Is the vitamin B1 needed for transamination reaction?
16.
Histidine in liver may deaminate by the mechanism of intramolecular deamination.
17.
The reduced coenzymes of amino acid oxidases may directly oxidated by molecular
oxygen.
18.
Glutamate deamination occurs through intermediate formation of imino acid.
19.
FAD is the coenzyme for monoaminoxidases (MAO).
20.
Decarboxylation of amino acids is the irreversible processes.
Topic 7
1. Amide nitrogen of glutamine may be used for heme synthesis.
2. Heme synthesis takes place in cell cytosol.
3. Acetyl-CoA is necessary for heme synthesis.
4. The direct bilirubin is mono- or diglucuronide of biliribin.
5. Indirect bilirubin inters into bile stones.
6. Iron for heme synthesis stores in the form of ferritin.
7. Does the heme synthesis regulated by the feedback type?
8. Is the δ-aminolevulinate synthase an allosteric enzyme?
9. Is the stercobilinogen formed in liver?
10. Is the bilirubin colored?
11. The nitrogen compounds of food are used for nucleic acid synthesis of our organism.
12. Glutamate is precursor of NH2 –group for GMP synthesis from imosinic acid.
13. The end product of adenosine degradation in human is uric acid.
14. The normal value of uric acid concentration in human blood is 0.2 g/l.
15. The regulation of pyrimidine bases is realized by the type of feed-back.
16. The nitrogen of pyrimidine bases is rexcreted from organism in the form or urea in
general.
17. Takes the asparagine part in the synthesis of purine ring?
18. May the CMP be synthesized from UMP?
19. Is the β–alanine the end product of TMP catabolism in human organism?
20. Takes the carbamoylphosphate part in the synthesis of pyrimidine nucleotides?
3. Tasks for an individual work
Topic 1
1.
2.
3.
4.
5.
6.
7.
8.
9.
Amino acids: their structure and properties. Classification of the amino acids.
Essential and nonessential amino acids.
Polypeptide chain.
The ways of natural peptides synthesis.
Examples of natural peptides: oxytocin, vasopressin, angiotensin, glutathione.
Structural features of the peptides, providing their resistance to proteolysis.
Amino acid composition of proteins. Color reactions of proteins.
Levels of protein structure: primary, secondary, tertiary and quaternary structure.
Relationship between the protein structure and biological function. The domain
structure of proteins.
10. Protein modification after the ribosomal synthesis (post-translational modification of
proteins).
11. Folding of protein molecules. Role of chaperones. Protein misfolding.
12. . Physico-chemical properties of proteins. The isoelectric point of the protein
solutions.
13. Functions of proteins in the body.
14. Methods of protein separation and purification: dialysis, fractionation,
electrophoresis, chromatography (gel-filtration, ion-exchange chromatography,
affinity chromatography).
Topic 2
1. Classification of the complex proteins (examples)
2. Nucleoproteins.The biological role. The chemical composition of nucleoprotein.
3. Chromoproteins. The biological role. Structure of hemoglobin. Hemoglobinopathies
and thalassemias. Cooperative binding of oxygen. Allosteric regulation.
4. Phosphoproteins. Biological role. Character of chemical bonds with phosphoric acid.
5. Chemical structure of nucleic acids. Primary, secondary and tertiary structure of DNA.
6. Ribosomal, information and transport RNAs. Their structure, distribution and
biological role.
7. Biological catalysts. Ribozymes. Enzymes.
8. The concept of the coenzyme. Coenzymes and vitamins.
9. Active sites of enzymes (catalytic and regulatory centers). Allosteric effectors.
Activators and inhibitors of enzymes.
10. General properties of enzymes: thermolability, pH-dependence, the specificity of
action. The concept of the rate of enzymatic reaction. Units of enzyme activity.
11. Relationship between the substrate concentration and the rate of enzymatic reactions.
The concept of the Michaelis constant.
12. Types of enzyme inhibition: competitive, noncompetitive inhibition and
uncompetitive. Lineweaver-Burk double-reciprocal plot.
13. Isoenzymes and their significance for medicine.
14. Classification of enzymes. Characteristic of each class of enzymes (examples).
15. Intracellular regulation of enzyme activity.
Topic 3
1. The concept of avitaminosis, hypo- and hypervitaminosis as diseases associated with
dysfunction of the enzyme systems.
2. Vitamins of group A. The structure and properties. The biological role. Food sources
of vitamin A. Absorption in the intestine. Provitamins. Hypo- and hypervitaminosis.
The daily requirement.
3. Vitamins of group D. Structure and properties. Provitamins, ergosterol, 7dehydrocholesterol. Dietary sources. The biological role. Hypo- and hypervitaminosis.
The daily requirement. Clinical application.
4. Vitamins of group E. Structure and properties. Hypovitaminosis. Dietary sources.
Clinical application.
5. Vitamins of group K. Structure and biological role. Clinical application.
6. Vitamin B1. The structure and properties. Coenzyme form. Role in metabolism.
Hypo- and hypervitaminosis. Dietary sources. The daily requirement. Clinical
application.
7. Vitamin B2. The structure and properties. Coenzyme forms. Role in metabolism.
Dietary sources. The daily requirement.
8. Vitamin B6. The structure and properties. Coenzyme forms. Hypovitaminosis. Dietary
sources. The daily requirement.
9. Vitamin B12. The chemical composition. Role in metabolism. Dietary sources. An
absorption of B12. Clinical application.
10. Vitamin C. Structure and properties. The biological role. Hypovitaminosis. Clinical
application. The daily requirement.
11. Biotin. The structure and properties. Hypovitaminosis. Dietary sources.
12. Vitamin PP. Structure. Coenzyme forms. Hypo- and avitaminosis. Dietary sources.
Role in metabolism. The daily requirement.
13. Folic acid. Structure. Distribution in nature. Participation in the construction of
coenzymes. Hypo- and avitaminosis.
14. Vitamin B3. Structure. The biological role. The daily requirement.
15. Chemistry of the lipids. The structure, classification, biological role, transport in the
body.
16. Glycerophospholipids and sphingolipids. Structure and biological role.
17. The biological role of sterols. The chemical structure of cholesterol.
18. Chemistry of fatty acids. Structure and biological role.
19. General presentation of hormones. Hierarchy of hormones.
20. The role of hormones in metabolism regulation. Mechanisms of hormonal signal
transduction. Examples of hormonal signal transduction by protein receptors. The
1.

3.
4.
5.
6.
7.
8.
9.
notion of G-proteins and second messengers. The intracellular and intranuclear
receptors. Regulation of transcription.
21. The hormones of the adrenal medulla. Their synthesis and breakdown. Mechanism of
action. Role in the regulation of metabolism.
22. Thyroid hormones. Their structure and formation in the body. Hypo- and
hyperthyroidism.
23. Pancreatic Hormones. Their chemical nature and the effect on metabolism. Insulin and
glucagon.
24. Hormones of steroid nature. Their structure and mechanism of action. Male and
female sex hormones.
25. The hormones of the adrenal cortex. The chemical nature and the effect on
metabolism. Mechanism of action.
26. The anterior pituitary hormones. The chemical structure of their biological effects.
Hypothalamic hormones. Structure and biological role.
Topic 4
1. General principles of energy and metabolism. Catabolism and anabolism are the basic
metabolic processes. Role of NADPH (H +) and ATP.
2. Monosaccharides, oligosaccharides. The most important representatives of
monosaccharides and oligosaccharides of the animal organism. Chemical structure,
biological role.
3. Polysaccharides. Glycogen, its structure and properties. How Glycogen Is Produced
and Degraded How does the breakdown of glycogen take place? How is glycogen
formed from glucose? How is glycogen metabolism controlled?
4. Anaerobic breakdown of carbohydrates, its biological significance. Energy effect.
Substrate level phosphorylation.
5. Glycolysis. Regulation. Energy effect.
6. Gluconeogenesis. Energetic effect of the process. Regulation.
7. Oxidative decarboxylation of pyruvic acid. Coenzymes and enzymes involved in this
process.
8. The citric acid cycle. Its biological significance. Regulation.
9. Links between TCA cycle and biological oxidation.
10. The Role of Electron Transport in Metabolism. Oxidative phosphorylation. Peter
Mitchell and Chemiosmotic theory. ATP synthesis.
11. Pentose phosphate pathway of glucose oxidation in tissues and its biological role.
12. Mechanisms of regulation of blood glucose. Hypoglycemia and hyperglycemia.
Diabetes. Diagnostic value of sugar curves.
13. Possible ways of glucose-6-phosphate conversions in the liver.
Topic 5
Peculiarities of absorption and transport of lipids.
Degradation and synthesis of triacylglycerols. Oxidation of glycerol.
-oxidation of fatty acid in mitochondria
Biosynthesis of fatty acids and phospholipids in different tissues.
Acetone bodies.
Biosynthesis of cholesterol
Links between lipid and carbohydrate metabolism. Central role of CoA in lipid
metabolism.
Regulation and pathology of lipid metabolism. Intracellular lipids and blood serum lipids.
Microsomal oxidation of lipids. Role of cytochrome P450 in xenobiotic
detoxification. Reactive oxygen species
Topic 6
1. Problem of nitrogen nutrition. Essential and nonessential amino acids. Digestion of
proteins in gastrointestinal system. Absorption and active transport of amino acids.
Protein putrefaction in the intestine (indole, skatole, phenol, cresol)
2. Pathways of amino acid metabolism. Deamination (oxidative and non-oxidative) and
transamination of amino acids. Role of the coenzymes in these reactions. Diagnostic
significance of the aminotransferases in the blood
3. The fate of α-keto acids. Glucogenic and ketogenic amino acids.
4. Synthesis and degradation of biogenic amines and their biological role. MAO
5. Notion on hydroxylation and methylation reaction. (Examples)
6. The ammonia detoxification pathways. Urea synthesis in the liver.
7. Metabolism of individual amino acids:
a. Gly, Ser,
b. Cys, Met,
c. Arg,
d. Glu, Asp,
e. Phe, Tyr, Trp
8. Biosynthesis of creatine phosphate and its physiological role.
9. Regulation and pathology of amino acids metabolism.
Topic 7
1. Sources of purine nucleus atoms . Biosynthesis of AMP and GMP from inosinic acid.
2. The degradation of purine nucleotides. Hyperuricemia and gout.
3. Basic synthesis reaction of the pyrimidine nucleotides.
4. The degradation of the pyrimidine nucleotides.
5. The biosynthesis of nucleic acids.
6. The biosynthesis of heme and its degradation. Determination of the direct and indirect
bilirubin in the blood serum.
7. Protein biosynthesis. The main components of the protein synthesis system. Posttranslational modification of the proteins.
8. Integration of the carbohydrate, lipids and proteins metabolism and its regulation.
9. Examples of enzymes in the medicine. (LDH, ALT, AST, Alkaline phosphatase, creatine
kinase and others)
10. Abnormal urine components.
11. Basic nitrogen-containing inorganic components of the urine.
12. The main chemical components of human serum.
Examples of the tests
Amino Acids and Simple Proteins
1 Essential for man amino acids are:
1 Phenylalanine
2 Tyrosine
3 Tryptophan
4 Threonine
5 Histidine
2 Which from the following amino acids
have the positive charge?
1 Asparagine
2 Glutamine
3 Lysine
4 Glutamate
5 Histidine
3 Sulphur containing amino acids are:
1 Methionine
2 Lysine
3 Valine
4 Cysteine
5 Arginine
4 Hydrophobic amino acids are:
1 Glutamine
2 Valine
3 Threonine
4 Phenylalanine
5 Isoleucine
5 Which from the following bonds do not
break during protein denaturation?
1 Disulphides
2 Hydrogens
3 Peptides
4 Ionics
5 Hydrophobics
6 The donator of methyl groups is:
1 Valine
2 Leucine
3 Methionine
4 Arginine
5 Threonine
7 The largest value of Rf for amino acid
during paper chromatography is for:
1 Glycine
8
9
10
11
2 Threonine
3 Serine
4 Glutamate
5 Valine
The isoelectric point of proteins depends
on the presence of:
1 Hydrate layer
2 Total charge
3 Hydrogen bonds
4 Helical parts in protein molecule
5 All of the above
The biuret reaction is positive for:
1 Simple proteins
2 Dipeptides
3 Tripeptides
4 Solution of amino acids
5 Gelatine
The main property of the oligomeric
proteins:
Penetrate through semipermeabile
1
membrane
2 Do not contain α-helical regions
3 Consist from several polypeptide chains
4 Do not possess the tertiary structure
5 All of the above
Hydrophilic amino acids are:
1 Glutamine
2 Serine
3 Arginine
4 Phen
5
l
a
l
a Asparagine
n
i
n
e
12 Amino acid without stereoisomeres is:
1 Tyrosine
13
14
15
16
17
18
19
2 Glysine
3 Alanine
4 Cysteine
5 Serine
Essential for man amino acids are:
20
1 Lysine
2 Threonine
3 Ornithine
4 Valine
5 Cysteine
Amino acids which are the derivatives of
propionic acid:
21
1 Alanine
2 Serine
3 Cysteine
4 Threonine
5 Phenylalanine
Hydrophobic amino acid is:
22
1 Serine
2 Leucine
3 Glutamine
4 Cysteine
5 Lysine
Protein denaturation may be achieved
by:
23
1 Concentrated nitric acid
2 Copper sulphate
3 Silver nitrate
4 Concentrated alkaline
5 Ammonium sulphate
24
The amino acid with thiol group is:
1 Aspargine
2 Histidine
3 Lysine
4 Cysteine
5 Metionine
Which pairs of the following amino acids 25
can not be separated by ion-exchange
chromatography?
1 Glutamate and Lysine
2 Glutamate and Leucine
3 Leucine and Lysine
4 Leucine and Valine
26
5 Valine and Glutamate
The denaturation of proteins always
accompany with the:
1 Destruction of tertiary structure
2 Hydrolysis of peptide bonds
3 Appearance of color
Formation of functional complexes with
4
other proteins
Elimination of native biological
5
properties
Which of the following bonds stabilize
the tertiary protein structure?
1 Esters
2 Hydrophobics
3 Hydrogens
4 Ions
5 Disulphides
The ninhydrin reaction is negative with:
1 Simple proteines
2 Dipeptides
3 Tripeptides
4 Free amino acids
5 Carbonic acids
Collagen contains the largest amount of
amino acid residues:
1 Histidine
2 Glycine
3 Asparagine
4 Leucine
5 Glutamate
Glutathione is a:
1 Amino acid
2 Dipeptide
3 Ttripeptide
4 Tetrapeptide
The derivative of succinate is:
1 Glutamate
2 Histidine
3 Proline
4 Tryptophan
5 Aspartate
Molecular mass of proteins may be
determined by:
1 Sedimentation analysis
2 Dialysis
3 Ion-exchange chromatography
4 Colorimetry
5 Gel-filtration
Albumines are soluble in:
1 Distilled water
2 Phosphate buffer, pH=6.8
3 Semisaturated ammonium sulphate
4 Semisaturated copper sulphate
5 Saturated ammonium sulphate
2 Primary structure of nucleic acids
3 Tertiary structure of proteins
27 The mixture of proteins with different
molecular masses may be separated by:
4 Tertiary structure of nucleic acids
1 Gel-filtration
30 Hydrophilic amino acids are:
Ultrafiltration through the filter with
1 Phenylalanine
2
different size of pores
2 Leucine
3 Dialyses
3 Threonine
4 Ultracentrifugation
4 Serine
5 Salting-out
5 Alanine
28 The positive xanthoprotein reaction is
typical for:
1 Phenylalanine
2 Methionine
3 Tryptophan
4 Arginine
5 Asparagine
29 Shaperons take part mainly in the
formation and stabilization of:
1 Primary structure of proteins
Conjugated Proteins, Nucleic Acids and Enzymes
1 Amylase belongs to the following class of
3 Pyrimidine
Enzymes:
4 Imidasole
1 Oxidoreductases
5 Pyridine
2 Hydrolases
6 The enzyme may be activated by:
3 Lyases
1 Substrate
4 Ligases
2 Allosteric inhibitor
5 Isomerases
3 Product of reaction
2 The Enzyme mixture can not be
4 Cofactor
separated by:
7 The specific activity of an enzyme means:
1 Precipitation
1 The amount of enzyme that produces 1
2 Dialysis
mol of product per second under
3 Gel Filtration
standard conditions
4 El
2 The activity of an enzyme in relation to a
standard preparation of the enzyme
5
3 The number of enzyme units per
c
milligram of protein
tr
4
The amount of enzyme causing
o
transformation of 1 μmol of substrate per
p
minute under standard conditionss
h
5 The activity of an enzyme in the
o
presence of its preferred substrate
r
e
8 An enzyme that catalyzes the synthesis of
si
organic substances using ATP hydrolisis
s
would be classified as:
1 Oxidoreductases
on-Exchange Chromatography
2 Transferases
3 Hydrolases
3 The Enzyme catalyzing interconversion
of ketoses and aldoses belongs to the class 4 Isomerases
5 Ligases
of:
9 Enzymes increase the rates of reactions
1 Oxidoreductases
by:
2 Transferases
1 Increasing the free energy of activation
3 Hydrolases
Increasing the free-energy change of the
4 Isomerases
2
reaction
5 Lyases
4 Cholinesterase catalyses the hydrolysis of 3 Changing the equilibrium constant of the
reaction
bonds:
4 Decreasing the energy of activation
1 Ester
10 The Michaelis constant (KM) is:
2 Glucosides
1 Numerically equal to Vmax/2
3 Peptides
The equilibrium constant for the
4 Disulfides
2
dissociation of ES to E + P
5 Hydrogens
Increased at the presence of non5 Heme molecule consist from four
3
competitive inhibitor
derivatives of rings:
The substrate concentration at which V
1 Pyrrole
4
is one-half of Vmax
2 Purine
11 Which of the following regulatory actions
involves a reversible covalent
modification of an enzyme?
1 Allosteric modulation
2 Competitive inhibition
18
Conversion of zymogen to active
3
enzyme
Association of apoenzyme with a
4
cofactor
Phosphorylation of the hydroxyl group in
5
the serine residues
19
12 The type of enzyme inhibition in which
KM increases but Vmax does not change is:
1 Competitive
2 Non-competitive
3 Irreversible
4 Uncompetitive
13 An allosteric effector changes the enzyme
activity by:
Competing for the catalytic site with the
1
substrate
Binding to a site on the enzyme molecule
2
20
distinct from the catalytic site
3 Precipitating of the enzyme molecule
4 None of the above
14 Catalase belongs to the class of enzymes:
1 Oxidoreductases
2 Transferases
21
3 Hydrolases
4 Lyases
5 Isomerases
15 … does not bind to the active site of
enzyme:
1 Substrate
2 Product
22
3 Coenzyme
4 Competitive inhibitor
5 Allosteric effector
16 The subunit number in lactate
dehydrogenase:
1
2
3
4
5
Two
Three
Four
Six
Eight
17 Kinases require:
1 Mn
2 Cu
3 Mg
Inorganic
4
phosphate
5 Zinc
Apoenzyme may be activated by:
1 Substrate
2 Allosteric activator
3 Product of reaction
4 Coenzyme
One enzyme unit means:
1Quantity of enzyme which catalyzes the
formation of 1 mole of the product per
second
Quantity of moles of the substrate,
2
undergo by 1 mol of enzyme per sec
Number of Enzyme units per 1 mg of
3
protein
4Quantity of enzyme which catalyze the
formation of 1 micromole of the product
per minute
5 Activity of enzyme to the best substrate
Сompetitive inhibitors:
1 Increase the KM enzyme
2 Decrease the KM enzyme
3 Increase Vmax
4 Decrease Vmax
5 Do not change KM and Vmax
Specificity of Holoenzyme depends from:
1 Coenzyme
2 Apoenzyme
3 Allosteric effector
4 Cosubstrate
5 All indicated factors
Which enzyme does not belong to
Oxidoreductases:
1 Catalase
2 Peroxidase
3 Cholinesterase
4 Ascorbate oxidase
5 Lactate dehydrogenase
23 Enzymatic Reaction rate accelerates by:
1 Decreasing the temperature
2 Increasing the enzyme quantity
3 Denaturation of enzyme
4 Coenzyme deficiency
5 Edition of allosteric activator
24 The substance with the catalytical
activity is:
groups in enzyme
1 Insulin
3 Change of substrates charge
2 Glucagon
4 Dissociation of enzyme
3 Casein
5 Denaturatin of enzyme
4 Pepsin
29 If the substrate concentration is equal to
5 Keratin
KM the reaction rate may be:
1 0.25 Vmax
25 Сompetitive inhibition may be reversed
by:
2 0.33 Vmax
1 Rising the temperature
3 0.50 Vmax
2 Adding the product of reaction
4 0.67 Vmax
3 Excessive substrate concentration
5 0.75 Vmax
4 Heav
30 Which proteins take part in a specific
metal ions
links and transport of iron?
1 γ-Globulins
26 Enzyme which belongs to
2 α-Globulins
Oxidoreductases:
3 Transferrins
1 Amylase
4 Ceruloplasmin
2 Tripsin
5 Albumins
3 Catalase
4 Cholinesterase
5 Pepsin
27 It is not Hemoprotein:
1 Myoglobin
2 Cytochrome c
3 Catalase
4 Hemoglobin
5 Casein
28 Changes of pH medium may lead to:
Break of peptide bonds in enzyme
1
molecule
2 Change of ionization of dissociated
Vitamins, Lipids and Hormones
1 The causes of hypovitaminoses may be
due to:
1 Deficiency of vitamin in food
2 Disturbance of vitamin transport
3 Disturbance of coenzyme synthesis
4 Genetic defect of apoenzyme
2 The vitamin with the maximum daily
requirement for human is:
1А
2 В1
3 РР
4D
5Е
3 The vitamins with heterocycles in their
structure are:
1 Tocopherol
2 Thiamine
3 Pyridoxine
4 Niacin
5 Pantothenic acid
4 The vitamins which are essential for
hydrogen transport:
1 Thiamine
2 Riboflavin
3 Folic ac
4
d Niacin
8
9
10
11
5 Biotin
5 The vitamin which is the component of
coenzyme A is:
12
1 Thiamine
2 Riboflavin
3 Pantothenic acid
4 Pyridoxine
5 Cobalamin
6 The characteristic symptom of Vitamin
PP deficiency:
13
1 Sclerosis
2 Rickets
3 Pellagra
4 Scurvy
5 Beriberi
7 Coenzyme is attached to enzyme:
14
1 In allosteric centre
2 Always in active site
3 By different chemical bounds
4 Tightly or not tightly
Gs-protein:
1 Contains three subunits
2 Is connected with GDP or GTP
3 Inhibits adenylate cyclase
4 Is a membrane protein
5 Activates DNA
The vitamin D deficiency in adults may
cause:
1 Osteomalacia
2 Xerophtalmia
3 Macrocytic anemia
4 Scurvy
5 Rickets
The Vitamins which do not contain the
heterocycles in their structure are:
1 Retinol
2 Pyridoxine
3 Cholecalciferol
4 Riboflavin
5 All indicated vitamins
The vitamin with the minimal daily
requirements for human is:
1A
2D
3C
4 PP
5E
The vitamin which is essential for NH2group transfer is:
1 Pyridoxine
2 Riboflavin
3 Thiamine
4 Ascorbic acid
5 Nicotinamide
Steroid hormones:
1 Penetrate into the cell
2 Bind with membrane receptors
3 Activate G-protein
4 Stimulate the mRNA synthesis
5 Participate in all indicated processes
NAD+ and NADP+ are coenzymes of
vitamin:
15
16
17
18
19
20
21
1P
2 PP
3K
22
4C
5 B3
The vitamins with antioxidant activity
are:
1Н
2 В6
3А
23
4Е
5С
Adenylatcyclase is:
1 A membrane enzyme
2 A cytoplasmic enzyme
24
3 Activated by Gs-protein
The enzyme which catalyzes the cAMP
4
synthesis
5 Containing heme
Which substance is a nucleotide?
1 Adenine
2 Adenine hydrolase
3 Cytidine
25
4 Prion
Adenosine
5
monophosphate
Essential fatty acids are:
1 Linoleic acid
2 Linolenic acid
26
3 Arachidonic acid
4 Oleic acid
5 Palmitic acid
Fat-soluble vitamins are:
1 Pyridoxine
27
2 Thyamine
3 Retinol
4 Philloquinone
5 Folic acid
Saturated fatty acid is:
1 Oleic acid
28
2 Linoleic acid
3 Linolenic acid
4 Palmitic acid
5 Arachidonic acid
Coenzyme of succinate dehydrogenase is:
1 NAD+
2 FAD
29
3 FMN
4 TPP
5 CoA
The requirement of what vitamin is
rising with aging and hard working?
1 B1
2 B2
3 B3
4 B6
5 B12
Which pair of vitamins contains sulfur
atom in their molecules?
1 Thiamine and Biotin
2 Thiamine and Folic acid
3 Pyridoxine and Biotin
4 Biotin and Riboflavin
Vitamin which is required for
carboxylation reaction is:
1 Thiamine
2 Biotin
3 Cobalamin
4 Pyridoxine
5 Ascorbic acid
Water-soluble vitamins are:
1 Retinol
2 Niacin
3 Cobalamin
4 Tocopheroll
5 Biotin
Nitric oxide(NO) is:
1 Bioactive molecule
2 Synthesized from lysine
3 Synthesized from arginine
4 Exert long effect
The steroid derivatives are:
1 Sex hormones
2 Glucocorticoids
3 Bile pigments
4 Cholesterol
5 All indicated substances
FAD and FMN are coenzymes of
vitamin:
1 B1
2 B2
3 B3
4 B6
5 B12
Which chemical substances are not a
component of biomembrane:
1 Glycerol
2 Cholesterol
3 Sphingomyelins
4 Phosphatidylcholines
5 Triacylglycerols
30 Calmodulin is:
1 Glycerophspholipid
2 Thyroid hormone
3 Intracellular Ca2+-binding protein
4 Precursor of calcitonine
5 No one from indicated substances
2 12
3 38
Chemistry and Metabolism of
4 15
Carbohydrates
5 72
8 The main function of pentose phosphate
1 Normal Glucose level in blood serum is:
pathway in erythrocyte is:
1 3.3-5.5 mmol/l
1 Synthesis of NADPH++H+
2 2.2-2.3 mmol/l
2 Synthesis of xylulose-5-phosphate
3 5.5-8.6 mmol/l
3 Splitting of pentose phosphates
4 2.0-6.6 mmol/l
4 Synthesis of ATP
5 10.5-11.0 mmol/l
5 Reduction of H2O2 to H2O
2 The end product of anaerobic glycolysis 9 Noninsulin-dependent Diabetes Mellitus
in muscle is:
occurs due to:
1 Pyruvate
1 Alteration of glycolysis regulation
2 Lactate
2 Increasing of insulin secretion
3 Oxaloacetate
3 Increasing of glucagon secretion
4 Ethanol
4 Decreasing of insulin secretion
5 Acetyl-CoA
5 Changes of insulin-dependent uptake of glucose
3 Normal values of glucose in blood serum10
are:The common stage of glycolysis
1 3-5 g/l
and gluconeogenesis, catalyzed
2 0.6-1.0 g/l
by common enzyme is:
3 3.3-5.5 mmol/l
1 Fru-6-ph
Glc-6-ph
4 60-100 mg/dl
2 Glc-6-ph
Glc
5 None from indicated
3 Oxaloacetate
Phosphoenolpyruvate
4 The content of pyruvate in blood
4 Fru-1,6-bisph
Fru-6-ph
is raised during the hypovitaminosis:
5 No one from indicated
1 A
11 The Enzyme which does not take part in CAC:
2 C
1 Aconitate hydratase
3 D
2 Transketolase
4 B1
3 Succinate dehydrogenase
5 B6
4 Fumarate hydratase
5 The Enzyme which limits the rate
5 Malate dehydrogenase
of glycolysis is:
12 Which enzymes of glycolysis catalyse
1 Glyceraldehyde phosphate dehydrogenase the irreversible reactions?
2 Enolase
1 Thriosophosphate isomerase
3 Phosphofructokinase
2 Aldolase
4 Phosphoglycerate kinase
3 Phosphofructokinase
5 Triosophosphate isomerase
4 Lactate dehydrogenase
6 Which products may be formed
5 Hexokinase
from Glucose-6-phosphate in one stage? 13 Lactose is degraded to:
1 Fructose-6-phosphate
1 Galactose and glucose
2 Glucose
2 Galactose and fructose
3 6-Phosphoglucone lactone
3 Glucose and mannose
4 Glucose-1-phosphate
4 Glucose and fructose
5 Fructose-1-phosphate
5 Only Glucose
7 The energetic value (ATP quantity)
14 Maltose is degraded to:
of pyruvate oxidation to CO2 and H2O:
1 Galactose and glucose
1 24
2 Galactose and fructose
15
16
17
18
19
20
21
3 Glucose and mannose
4 Glucose and fructose
5 Only Glucose
22
Sucrose may be splited only in:
1 Brain
2 Liver
3 Muscle
4 Intestine
5 Kidney
23
Which monosaccharide is formed
during full hydrolysis of glycogen?
1 D-Fructose
2 Fructose-6-phosphate
3 Glucose-6- phosphate
4 D-Glucose
5 Fructose-1,6-bisphosphate
24
In which C-atom of pyruvate
14
will appeared C-1 of Glucose?
1 1
2 2
3 3
4 In all atoms
5 None of atoms
25
The substrate phosphorylation
takes place in the course of:
1 Glycolysis
2 Gluconeogenesis
3 Glycogenolysis
4 Pentose Phosphate pathway
5 CAC
26
The major quantity of Glycogen
in the organism is in:
1 Liver
2 Muscles
3 Brain
4 Kidney
27
5 Adipose tissue
Which substances are allosteric regulators?
1 AMP
2 ATP
3 Fructose-6-phosphate
4 Citrate
28
5 Pyruvate
In which reaction of CAC the hydratation
is occurs?
1 α-Ketogutarate
Succinyl-CoA
2 L-Malate
Oxaloacetate
3 Succinate
Fumarate
4 Fumarate
L-Malate
5 Isocitrate
α-Ketoglutarate
Which metabolic pathways supply
the sugars for nucleic acid synthesis?
1 Glycolysis
2 Gluconeogenesis
3 Glycogenolysis
4 CAC
5 Penthose Phosphate pathway
In patients with diabetes the hyperdose
of insulin may lead to:
1 Glucosuria
2 Galactosemia
3 Hyperglycemia
4 Hypoglycemia
5 Creatinuria
Which enzyme participates in the formation
of Glucose-1-phosphate from glycogen?
1 Amylase
2 Phosphorylase
3 Phosphoglucoisomerase
4 Phosphoglucomutase
5 Glucokinase
The net yield of ATP during CAC
(without oxidative phosphorilation) is:
1 0
2 1
3 2
4 38
5 12
Glucose may be formed in the organism from:
1 Acetyl-CoA
2 Pyruvate
3 Lactate
4 Glycerol
Enzymes which catalyze the glycogen synthesis
from glucose are:
1 Amylase
2 Phosphorylase
3 Glycogen synthase
4 Phosphoglucomutase
5 Glucokinase
The rate of glycolysis in muscle is diminished
in the presence of:
1 ADP
2 ATP
3 Citrate
4 AMP
29 The products which are formed from
Pyruvate in one step are:
1 Citrate
2 Oxaloacetate
3 Lactate
4 Acetyl-CoA
5 Glycerol
30 Enzyme which is present both in liver
and in muscle is:
1 Glucose-6-phosphatase
2 Hexokinase
3 Fructose-1,6-bisphosphatase
4 Pyruvate carboxylase
5 Glucokinase
Lipid metabolism
1 Saturated fatty acids are:
1 Oleic
2 Arachic
3 Palmitoleic
4 Palmitic
5 Arachidonic
2 Which of the following substances are
the derivatives of cholesterol?
1 Vitamin D3
2 Vitamin A
3 Bile acids
4 Corticosteroids
5 Prostaglandins
3 Unsaturated fatty acids are:
1 Palmitic
2 Oleic
3 Stearic
4 Arachic
5 Arachidonic
4 The allosteric enzyme which regulates
the fatty acids synthesis in cytosol:
1 Acetyl-CoA carboxylase
2 Hexokinase
3 Phosphofructokinase
4 Citrate synthase
NADP +-dependent β-hydroxy- β5
methylglutaryl-CoA
8
9
10
11
eductase
5 The content of triacylglycerols in
chylomicrons (in %) is approximately:
1 10
2 20
3 30
4 50
5 80
6 Which substance participates in fatty
acids transport from cytosol into
mitochondria?
1 Ornithine
2 Carnitine
3 Taurine
4 Creatine
5 Albumin
7 The participants in the biosynthesis of
12
13
fatty acids are:
1 Carnitine
2 Biotin
3 Sphingosine
4 Cerulopasmin
5 NADPH(H+)
Which substance participates in
phosphatidylserine synthesis?
1 Lecithin
2 CDP-diacylglycerol
3 Leucine
4 S-Adenosylmethionine
5 Sphingosine
Which substances are the components of
biomembrains?
1 Diacylglycerol
2 Free fatty acids
3 Cholesterol
4 Phospholipids
5 Glycolipids
Recirculation between liver and intestine
is typical for:
1 Phospholipids
2 Monoacylglycerols
3 Glycerol
4 Lysophospholipids
5 Bile acids
The antiatherogenic property is typical
for:
1 Chilomicrons
2 HDL
3 LDL
4 VLDL
5 Cholesterol esters
In mitochondria takes place:
1 The fatty acid β-oxidation
2 Citrate synthesis
3 Triacylglycerol lipolysis
4 Phospholipids biosynthesis
5 Synthesis of ketone bodies
Eicosanoids are formed from
arachidonic acid through:
1 Isomerisation
2 Methylation
3 Decarboxylation
Entherocytes?
4 Carboxylation and hydrolysis
Cyclooxygenase and lipoxygenase
1Triacylglycerols
5
pathways
2 Fatty acids
14 The triacylglycerols lipolysis in the fat
3 Bile acids
tissue is inhibited by:
Ketone
4
1 Insulin and Prostaglandins
bodies
2 Catecholamines
Phospholipid
5
s
3 Mineralcorticoids
21
The
main metabolic pathway of fatty
4 Glucocorticoids
acids in tissues is:
5 Glucagon
1 Chylomicron biosynthesis
15 The ketone bodies synthesis takes place
2 β-Oxdation
in:
3 Lipid transport
1Cytosol
4 Cell membranes construction
2 Mitochondria
5 Binding of metal ions
3 Nucleus
22 Acetyl-CoA carboxylase is inhibited by:
Goldgy
4
1 Citrate
complex
2 ATP
5 Microsomes
3 Mn2+
16 The substances which are the most active
4 Palmitic asid
in fat emulsification in intestine:
5 Biotin
Bile acids salts, unsaturated fatty acids
1
Substances
that inhibit the lipolysis in fat tissue are:
23
and monoacylglycerols
1 Thyroid hormones
2 Bile pigments and bile acids
2 Insulin, Prostaglandins
3 Organic and mineral acids
3 ACTH, Somatotropin
4 Cholesterol and steroid hormones
4 Catecholamines
5 Fat-soluble vitamins
5 Glucocorticoids
17 The coenzymes that take part in β24 The ketone bodies are:
oxidation of fatty acids are:
+
1 Acetyl-CoA, Succinyl-CoA
1 NAD
+
2 Acetoacetate, β-hydroxybutyrate
2 NADP
3 Acetoacetyl-CoA, Propionyl-CoA
3 FAD
4 Fumarate,Pyruvate, Malate
4 Coenzyme A
5 Oleate, Palmitate, Stearate
5 THF
18 To the group of Eicosanoids belong:
25 Acetyl-CoA takes part in the synthesis
1 Prostaglandins
of:
2 Prostacyclins
1 Glycerol
3 Thromboxanes
2 Cholesterol
4 Leucotrienes
3 Pyruvate
5 Isoprenoids
4 Acetoacetate
19 Which substance takes part in
5 Fatty acids
phosphatidylcholine biosynthesis by
26 The coenzyme which is essential for
methylation reaction?
biosythesis of cholesterol and fatty acids
1 Cholesterol
is:
2 B12
1 NADH(H+)
3 S-Adenosylmethionine
2 FADH2
4 Biotin
3 NADPH(H+)
5 N5-Methyl-THF
4 Vitamin H (Biotin)
20 Which substances are resynthesized in
5 Pyridoxal phosphate
4 Thyroxin, Glucocorticoids
5 Hypothalamic hormones
27 Succinyl-CoA is formed in the course of:
1 Fatty acid β-oxidation
30 Which substance acts as allosteric
activator in fatty acid synthesis?
2 Arachidonic acid oxidation
1 NADPH(H+)
3 CAC
2 Palmitic acid
4 Fatty acid biosynthesis
3 CO2
5 Sphingolipid biosynthesis
4 Citrate
28 The precursor of Eicosanoids is:
5 Avidin
1 Palmitate
2 Arachinate
3 Arachidonate
4 Stearate
5 Oleate
29 Hormones that activate the lipase in
adipocytes are:
1 Adrenaline, Noradrenaline
2 Prostaglandins, Insulin
3 Oxytocin, Vasopressin
Amino acid metabolism
1 The amino acid which participates in
detoxification of ammonia is:
1 Histidine
2 Asparagine
3 Glutamate
4 Glycine
5 Tryptophan
2 The coenzyme of glutamate
dehydrogenase is:
1 НАД+
2 Pyridoxal phosphate
3 FAD
4 FMN
5 Coenzyme Q
3 Phenylketonuria is developed due to
enzyme deficiency of classes:
Supply the synthesis of biological
amines
2 Demands the participation of PLP
3 Supply the essential amino acid synthesis
4 Is the ammonia liberation reaction
Leads to the elevation of amino acid
5
levels in tissue
The substances which do not participate
in urea formation cycle are:
1 Citrulline
2 Ornithine
3 Succinate
4 Arginine
5 Asparagine
To mixture (both ketogenic and
glucogenic) amino acids belong:
1 Alanine
2 Glycine
3 Phenylalanine
4 Serine
5 Leucine
Tetrahydrofolate participates in the
synthesis of:
1 Serine from Glycine
2 Citrulline from Ornithine
3 Tyrosine from Phenylalanine
4 Glutamate from Hisidine
5 Glutamine from Glutamate
Amino acids which do not participate in
transamination reaction are:
1 Glutamine and Asparagine
2 Lysine and Threonine
3 Isoleucine and Tyrosine
4 Phenylalanine and Tyrosine
5 Alanine and Valine
The NH3 in brain tissues is neutralized
through:
1 Synthesis of urea
2 Formation of NH4Cl
3 Convertion of Glutamate to Glutamine
4 Alanine formation
5 Creatine synthesis
The coenzyme of majority amino acid
decarboxylases is:
1 FAD
1
8
9
1Oxidoreductases
2 Transferases
3 Hydrolyses
4 Lyases
5 Isomerases
4 The daily excretion of creatinine in urine 10
is:
1 0.1-0.2 g
2 1.0-2.0 g
3 10-20 g
4 1.0-2.0 mg
5 10-20 mg
5 Inherited deficiency of the homogentisate 11
1,2-dioxygenase leads to the development
of:
1 Phenylketonuria
2 Parkinsone disease
3 Alkaptonuria
4 Albinism
12
5 Homocystinuria
6 Which amino acid participates in
creatine synthesis?
1 Valine
2 Leucine
3 Methionine
4 Serine
13
5 Threonine
7 The process of amino acid
transamination:
14
15
16
17
18
19
20
2 FMN
3 Pyridoxal phosphate
4 TPP
5 Biotin
Histidase belongs to the class of enzyme:
1 Oxidoreductases
2 Transferases
3 Hydrolases
4 Lyases
5 Isomerases
Skatole and Indole are formed by
intestinal microflora action from:
1 Tyrosine
2 Triptophan
3 Histidine
4 Phenylalanine
5 Proline
Pyridoxal phosphate is a coenzyme of:
1 Alanine aminotransferase
2 Glycogen phosphorylase
3 Aspartate aminotransferase
4 Amino acid Decarboxylase
The CAC metabolite which participates
in transamination reaction is:
1 Citrate
2 Isocitrate
3 Succinate
4 Fumarate
5 Oxaloacetate
γ-aminobutirate is formed from:
1 Histidine
2 Aspartate
3 Glutamate
4 Glutamine
5 Asparagine
The normal human urea value in daily
urine is:
1 25-35 mg
2 0.25-0.35 g
3 2.5-3.5 g
4 25-35 g
5 250-350 g
Glycine may be formed from:
1 Methionine
2 Lysine
3 Valine
4 Tyrosine
21
22
23
24
25
26
27
5 Serine
Nitric oxide (II) is formed from:
1 Arg
2 Cys
3 Val
4 His
5 Ser
Albinism is connected with the abnormal
metabolism of:
1 Methionine
2 Serine
3 Cysteine
4 Tyrosine
5 Tryptophan
The coenzyme of L- amino acid oxidase
is:
1 FMN
2 Pyridoxal phosphate
3 NAD+
4 NADP+
5 CoA
The activity of aspartate
aminotransferase in blood serum is
suddenly increased under:
1 Myocardial infarction
2 Pancreatities
3 Prostatities
4 Nephrites
5 Stomach diseases
HCl in Stomach participates in:
1 Protein denaturation
2 Antibacterial action
3 Activation of pepsinogen
Providing of an optimal pH medium for
4
pepsin action
5 Inhibition of pepsinogen
Coenzyme of monoamine oxidase (MAO)
is:
1 NAD+
2 FAD
3 NADH(H+)
4 TPP
5 Pyridoxal phosphate
Kwashiorkor (a children disease) is
observed during the deficiency in food:
1 Carbohydrates
2 Lipids
3 Proteins
4 Vitamins
5 Inorganic substances
28 Taurine is formed from:
1 Leucine
2 Cysteine
3 Glycine
4 Serine
5 Threonine
29 Ketogenic amino acid is:
1 Leucine
2 Cysteine
3 Alanine
4 Glycine
5 Threonine
30 Monooxygenases participate in the
synthesis of:
1 Tyrosine
Dihydroxyphenylalani
2
ne
3 Noradrenaline
4 5-Hydroxytryptophan
5 Asparagine
Synthesis of protein, DNA, RNA. Metabolism of Conjugated Proteins
1 The elevation of alkaline phosphatase
activity in plasma takes place during
pathology of tissues:
1 Muscle
2 Liver
3 Bones
4 Pancreas
5 Prostate
2 Cardiac enzymes are:
1 CPK
2 LDH
3 AsAT
4 Amylase
5 Alkaline phosphatase
3 Which from indicated enzymes in blood
serum are used as diagnostic tools?
1 Amylase
2 Pepsine
3 Rennine
4 Creatine phosphokinase
5 Catalase
4 Normal urine does not contain the
substance:
1 Urea
2 Creatinine
3 Creatine
4 Uric acid
Ammonium
5
salts
5 Which enzymes are used as drugs?
1 Pepsine
2 Trypsine
3 Chymotrypsine
4 Collagenase
5 Asparaginase
6 The lactate dehydrogenase (LDH) levels
in blood serum are increased in:
1 Myocardial infarction
2 Acute pancreatitis
3 Diabetes mellitus
4 Acute glomerulonephritis
5 All of above
7 The main pathway for ATP synthesis
from ADP in liver is:
1 Reaction with GTP
2 Oxidative phosphorylation
8
9
10
11
12
13
14
3 Substrate phosphorylation
4 Reaction with Pi
5 Reaction with CTP
The precursors for UMP synthesis are:
1 Carbamoylphosphate and Aspartate
2 Nicotinamide and Glutamate
3 Inosinic acid and Aspartate
4 Thymidine and Phosphate
5 Thymine and Ribose
The pyrimidine nitrogen is excreted from
the organism primarily in the form of:
1 Uric acid
2 Creatinine
3 Ammonium salts
4 Urea
5 Creatine
δ-Aminolevulinic acid is synthesized
from:
1 Succinyl-CoA and Glycine
2 Aspartate and Carbamoylphosphate
3 Aspartate and Glycine
4 Glutamate and Glycine
5 Acetyl-CoA and Oxaloacetate
The activated amino acids can links with:
1 Pseudouridylic loop of tRNA
2 mRNA codon
3 tRNA anticodon
OH-group of 3'-adenosine of the end
4
tRNA nucleotide
5 Phosphate of 5'end nucleotide of tRNA
The postsynthetic modification of
proteins may include:
1 Phosphorylation
2 Hydroxylation
3 Limited proteolysis
4 Covalent binding with prostetic group
Heme is a component of:
1 Amylase
2 Peroxidase
3 Pepsin
4 Myoglobin
5 Cytochromes
The blood buffer system includes:
1 Bicarbonate
2 Phosphates
15
16
17
18
19
20
21
3 Proteins
4 Hemoglobin
The sourse of NH2-group in the synthesis
of AMP from inosinic acid is:
22
1 Urea
2 Aspartate
3 Asparagine
4 Carbamoylphosphate
5 Ammonium salts
The direct substrates for DNA synthesis 23
are:
Deoxyribose, phosphate and nucleic
1
bases
2 Phosphate and deoxynucleosides
3 Deoxynucleoside triphosphates
4 Deoxynucleoside diphosphates
24
5 Purine and pyrimidine bases
The end product of TMP catabolism in
human is:
1 Uric acid
2 β-Aminoisobutyric acid
3 Inosinic acid
4 Creatine
25
5 β-Alanine
Adenine is a component of:
1 FAD
2 NAD+
3 CoA
4 PLP
26
5 Biotin
The Inosinic acid in the organism is the
precursor for synthesis of:
1 AMP
2 GMP
3 UMP
4 CMP
27
5 All indicated substances
UMP is a component of:
1 tRNA
2 mRNA
3 DNA
4 rRNA
28
5 Mitochondrial DNA
The amino acid which is formed in
protein molecule as a result of
postsynthetic modification is:
1 β-Alanine
2 Glycine
3 5-Hydroxylysine
4 Glutamine
5 Proline
The distinguish peculiarities of tRNA
include the presence of:
1 Anticodon
2 Adenosine on the 3'-end
3 Tertiary structure (conformation)
4 Large amount of minor nitrogen bases
The transcription of mRNA may be
regulated by:
1 Adrenalin
2 Noradrenalin
3 Cortisol
4 Vasopressin
The direct donor of methyl group in the
TMP synthesis:
1 Methionine
2 Methylmethionine
3 S-Adenosylmethionine
4 N5, N10 - CH2 - THF
5 Choline
In the course of myocardial infarction the
positive enzyme tests in blood includes:
1 Elevation of AST and ALT activity
2 Increase of LDH1 and LDH2
3 Elevation of Creatine kinase activity
Elevation of MB isoenzyme of creatine
4
kinase
Which components of urine are not
patological?
1 Proteins
2 Ketone bodies
3 Glucose
4 Sulphates
5 Bilirubin
Orotate is a precursor for synthesis of:
1 Purine nucleotides
2 Pyrimidine nucleotides
3 Heme
4 Cholesterol
5 Ketone bodies
The source of NH2-group in the synthesis
of GMP from inosinic acid is:
1 Aspartate
2 Glutamine
3 Glutamate
4 Carbamoylphosphate
5 Urea
29 The elevated level of acid phosphatase
activity in blood serum indicates on
disease of:
1 Heart
2 Muscle
3 Liver
4 Pancreas
5 Prostate
30 The conversion of dUMP into dTMP
requires the coenzyme:
1 Positively charged amino acids are:
1. Asparagine
2. Glutamine
3. Lysine
4. Glutamate
5. Histidine
2 Which bonds do not splited during
denaturation of protein?
1. Disulphide
2. Hydrogen
3. Peptide
4. Ionic
5. Hydrophobic
3 Biuret reaction will be positive with
following substances:
1. Simple proteins
2. Dipeptide
3. Tripeptide
4. Amino acid solution
5. Gelatine
4 Tertiary structure of proteins is stabilised
bythe following bonds:
1. Ether
2. Hydrophobic
3. Hydrogen
4. Ionic
5. Disulphide
5 What amino acid is the most abundant in
the collagen molecule?
1. Histidine
2. Glycine
3. Asparagine
4. Leucine
1
2
3
4
5
6
7
NAD+
FAD
THF
PLP
THB
5. Glutamate
Amilase belongs to the class of enzyme:
1. Oxidoreductases
2. Hydrolases
3. Lyases
4. Synthetases
5. Isomerases
Which from presented substances is a
nucleotide?
1. Adenine
2. Adenosine
3. Cytidine
4. Prion
5. Adenosine monophosphate
8
The substances which do not bond with
active site of enzyme:
1. Substrate
2. Product
3. Coenzyme
4. Competitive inhibitor
5. Allosteric effector
9
The nucleic acids are distinguished from
proteins by means of:
1. They are high molecular
substances
2. They have complicated tertiary
structure
3. They absorbe the light in
ultraviolet region
4. They do not contain amino acid
residues
10 Which substance does not belong to
natural minor nucleotides?
1. Methylcytidine phosphate
2. Hydroxymethylcytidine
phosphate
3. Dihydrouridine phosphate
4. Pseudouridine phosphate
5. Uridine phosphate
11 The vitamin with the highest daily
requirements for man:
1. A
2. B2
3. C
4. D
5. E
4. 60-100 mg/dl
5. No one from indicated values
17 Insulin independent diabetes mellitus
occurs due to:
1. Disturbances of glycolysis
regulation
2. Elevated insulin secretion
3. Elevated glucagone secretion
4. Reduced insulin secretion
5. Disturbances of insulindependent uptake of glucose
18 Hyperglycemia is observed under:
1. Tumor diseases of adrenal
cortex
2. Hyperfunction of thyroid gland
3. Kidney diseases
4. Diabetes mellitus
12 Coenzyme is linked with apoenzyme:
1. In allosteric centre
2. In active centre
19 The enzymes which catalyze the
3. By means of different chemical
irreversible glycolytic reactions:
bonds
1. Phosphoglycerate kinase
4. Always tightly
2. Enolase
3. Phosphofructokinase
13 The vitamins, which do not contain the
4. Lactate dehydrogenase
heterocycles in their structure:
5. Hexokinase
1. Retinol
2. Pyridoxine
20 The primer product formed during
3. Cholecalciferol
glycogen splitting in muscle:
4. Riboflavin
1. UDP-glucose
5. All indicated vitamins
2. Glucose-1-phosphate
3. Glucose-6-phosphate
14 The specificity of holoenzyme is
4. Fructose-6-phosphate
determined by:
5. Glucose
1. Lipid prosthetic group
2. Carbohydrate prosthetic group 21 Allosteric enzyme which regulates the
3. Apoenzyme
synthesis of fatty acids:
4. Coenzyme
1. Acetyl-CoA-carboxylase
5. All of the above
2. Thiolase
3. Phosphofructokinase
15 Which hormones act through G-proteins?
4. Lipase
1. Adrenaline
5. HMG-synthase
2. Noradrenaline
3. Triiodothyronine
22 Recirculation between liver and intestine
4. Hydroxycortisone
is typical for:
5. Glucagone
1. Phospholipids
2. Monoglycerols
16 The normal glucose level in man blood:
3. Glycerol
1. 3-5 g/l
4. Lysophospholipids
2. 0.6-1.0 g/l
5. Bile acids
3. 3.3-5.5 mmol/l
23 Into lymphatic system of intestine are
absorbed:
1. Chilomicrones
2. LDLP
3. HDLP
4. VLDLP
5. LDLP and VLDLP
24 Phospholipids:
1. Lecithins
2. Cardiolipins
3. Acylglycerols
4. Ceramide
25 Precursor for prostaglandins:
1. Palmitate
2. Arachinate
3. Arachidonate
4. Stearate
5. Oleate
26
27
28
29
30 The substances which are formed from
tyrosine
1. γ-Aminobutirate
2. Adrenaline
3. Noradrenaline
4. Dopamine
5. Phenylalanine
31 The activated amino acids are linked with:
1. Pseudouridylic loop of tRNA
2. mRNA codon
3. tRNA anticodon
4. 3-OH-group of ribose in final
adenosine of tRNA
5. Phosphate on 5’-end of tRNA
32 Heme is a component of:
1. Amylase
2. Peroxidase
3. Pepsin
In detoxification of ammonia take part the
4. Myoglobin
amino acids:
5. Cytochromes
1. Histidine
2. Aspartate
33 The end catabolic product of TMP in man:
3. Glycine
1. Uric acid
4. Glutamate
2. β-Aminoisobutyric acid
5. Tryptophan
3. Inosinic acid
4. Creatine
In creatine synthesis take part:
5. β-Alanine
1. Arginine
2. Leucine
34 The distinguished peculiarities of tRNA
3. Methionine
are the presence of:
4. Serine
1. Anticodon
5. Glycine
2. Adenosine at 3’-end
3. Large amounts of minor
The Substances that do not participate in
nitrogen bases
transamination:
4. Only deoxyribonucleotides
1. Glutamine and Asparagine
2. Lysine and Threonine
35 -Aminolevulinate is the intermediate
3. Isoleucine and Aspartate
during synthesis of:
4. Phenylalanine and Tyrosine
1. Purines
5. Alanine and Valine
2. Pyrimidines
3. Heme
Scatol and indol are detoxificated in liver
4. Cholesterol
by:
5. Ketone bodies
1. Glycine
2. Glutamate
36 Protein degradation in cells takes place in:
3. α-Ketoglutarate
1. Proteasomes
4. Uridine diphosphoglucuronic
2. Lysosomes
acid
3. Peroxysomes
5. Proline
4. Nucleus
5. Ribosomes
37 Establish the correlation between:
1
2
3
4
5
Glyceraldehyde
Pyruvate
Starch
Sacharase
Maltose
A
B
C
D
E
Polysaccharide
Disaccharide
α-Keto acid
Triose
Enzyme
38 Oxaloacetate is:
1. α-Keto acid
2. Pyruvate decarboxylation product
3. Biogenic amine
4. CAC metabolite
39 Establish the correlation between:
1
2
3
4
5
Alanine
Serine
Lysine
Aspartate
Tyrosine
A
B
C
D
E
Nonpolar amino acid
Polar uncharted amino acid
Polar negatively charged amino acid
Aromatic amino acid
Polar positively charged
40 The substance what does not belong to the steroid hormones:
1. Progesterone
2. Cortisol
3. Aldosterone
4. Testosterone
5. Calcitonine
41 Establish the correlation between:
1
Pepsin
2
Ribosome
3
Cytochrome c
4
Casein
5
Immunoglobulin
A
B
C
D
E
Hemoprotein
Nucleoprotein
Phosphoprotein
Glycoprotein
Simple protein
42 Isoelectric point of protein means:
1. The freezing point of water
2. The pH value optimum for enzyme action
3. The temperature optimum for enzyme action
4. The pH value under which the common charge of protein molecule is zero
5. No one of indicated states
43 The substance what contains CH3- end is:
1. Oxaloacetate
2. Pyruvate
3. Acetyl-CoA
4. Malate
5. Citrate
44 Establish the correlation between:
1 Acetone
A
2 Acetoacetate
B
3 βHydroxybutyrat
e
4 Pyruvate
C
5 Oxaloacetate
E
D
45 Establish the correlation between:
1
Serine
2
Cysteine
3
Methionine
4
Glutamine
5
Histidine
A
B
C
D
E
Thiomethyl group
Imidasole group
Amide group
Sulfhydryl group
Hydroxyl group
46 Pantothenic acid is a component of:
1. HS-CoA
2. CoQ
3. NAD+
4. NADPH(H+)
5. FAD
47 Cyclopentanoperhydrophenanthrene is a component of:
1. Ubiquinone
2. Tocoferols
3. Phylloquinone
4. Corticosteroids
5. Androgens
48 Name the following substance:
H
C
HO
H3C
O
CH2
O
PO3H2
N
1.
2.
3.
4.
5.
FMN
TPP
PLP
FAD
NAD
49 The metabolites of pentose phosphate pathway:
1. Pyruvate
2. Citrate
3. Glucose-6-phosphate
4. Ribulose-5- phosphate
5. Glucose-1-phosphate
50 Establish the correlation between:
1
2
3
4
Carbamoyl phosphate
Glycine
Dopamine
Serotonine
5 α-Ketoglutarate
A
B
C
D
E
Adrenaline synthesis
Creatine synthesis
CAC
Decarboxylation
of 5-hydroxytryptophan
Urea synthesis
51 Coenzyme of dehydrogenases may be:
1. NAD+
2. FAD
3. Pyridoxine
4. Biotin
5. CoA
52 Accumulation of acetyl-CoA in mitochondria will:
1. Accelerate the oxidative decarboxylation of pyruvate
2. Activate the gluconeogenesis
3. Inhibit the oxidative decarboxylation of pyruvate
4. Inhibit the gluconeogenesis
53 Establish the correlation between:
1 Accelerate lypolysis
2 Inhibit lypolysis
A
B
Catecholamines
Prostaglandins
54 The regulatory enzyme NH3-dependent carbamoylphosphate synthetase catalyzes the
reaction:
1. Which requires the spend of 1 molecule of ATP
2. Which requires the spend of 2 molecule of ATP
55 Establish the consequence of action among the participants of hormonal signal transduction:
1
A
cAMP
2
B
G-protein
3
C
Adenylate cyclase
4
D
Membrane receptor
5
E
Hormon
56 In blood of patient the glucose level was find the 2.9mmol/l. What sort of reasons might
be?
1. High consumption of glucose
2. Overdose of insuline
3. Stress
4. Starvation
57 The Trommer reaction allows to detect:
1. Glucose
2. Riboso-5-phosphate
3. Starch
4. Sucrose
5. Ribose
58 Find the correlation between X (figure) and Y (letter) in the following chemical reactions:
Dihydroxy-acetone phosphate  X
1,3- Bisphosphoglycerate
1
Glyceraldehyde
A
Triosophosphate isomerase
2
2-Phosphoglycerate
B
Phosphoglycerate kinase
3
3-Phosphoglycerate
C
4
5
2,3-Bisphosphoglycerate
Glyceraldehyde-3phosphate
D
E
Glyceraldehyde phosphate
dehydrogenase
Aldolase
Phosphoglyceromutase
59 Find the correlation between the processes and its graphical representation:
1
A.
B.
C.
D.
2
3
Dependence between OD and substrate concentration
Dependence between the rate of enzymatic reaction and temperature
Kinetics of lipase action
Sugar curve (normal)
60 Urea cycle was discovered:
1. L. Paster
2. H. Krebs
3. A.E. Braunstein
4. V.A. Engelhardt
5. A. Meister
Answers
Amino Acids and Simple Proteins
1.
2.
3.
4.
5.
6.
7.
4
1, 3, 4, 5
3, 5
1, 4
2, 4, 5
3
3
5
19.
20.
21.
22.
23.
24.
25.
1, 5
2, 3, 4, 5
5
2
3
5
1, 5
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
2
1, 3, 5
3
1, 2, 3, 5
2
1, 2, 4
1, 2,3, 5
2
1, 2, 3, 4
4
4
26.
27.
28.
29.
30.
1, 2, 3
1, 2, 4, 5
1, 3
3
3, 4
Conjugated Proteins, Nucleic Acids and Enzymes
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
2
2
4
1
1
1,4
3
5
4
4
5
1
2
1
5
3
3
4
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
4
1
2
3
2,5
4
3
3
5
2,3,4,5
3
3
Vitamins, Lipids and Hormones
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
1,2,3,4
3
1,2,3,4
2,4
3
3
2,3,4
1,2,4
1
1,3
2
1
1,4
2
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
3,4
4
2
2
1
2
2,3,5
1,3
1,2,4
2
1,5
3
15.
16.
17.
18.
3,4,5
1,3,4
5
1,2, 3
Chemistry and Metabolism of Carbohydrates
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
1
2
2,3,4
4
3
1,2,3,4
4
1
5
1
2
3,5
1
5
4
4
3
1, 3, 5
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
2
1,2,4
4
5
4
2
2
2,3,4
3,4,5
2,3
2,3,4
2
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
3
1,5
2
4
2
2
2,4,5
3
3
3
1
4
Lipid metabolism
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
2,4
1,3,4
2,5
1
5
2
2,5
2
3,4,5
5
2
1,2,5
5
1
2
1
1,3,4
1,2,3,4
Amino acid metabolism
1.
3
19.
4
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
1
1
2
3
3
2
3,5
3
1
2
3
3
4
2
1,2, 3,4
5
3
5
1
4
1
1
1,2,3,4
2
3
2
1
1,2,3,4
Synthesis of protein, DNA, RNA. Metabolism of Conjugated Proteins
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
2,3
1,2,3
1,4,5
3
1,2,3,4,5
1
2
1
4
1
4
1,2,3,4
2,4,5
1,2,3,4
2
3
2
1,2,3
1,2
1,2,4
3
1,2,3,4
3
4
1,2,3,4
4
2
2
5
3
Example for Examination Test
1
2
3
4
5
6
7
8
9
10
3,5
3
1,3,5
2,3,4,5
2
2
5
2,5
4
5
21
22
23
24
25
26
27
28
29
30
1
5
1
1,2
3
2,4
1,3,5
2
4
2,3,4
41
42
43
44
45
46
47
48
49
50
1E,2B,3A,4C,5D
4
2,3
1B,2C,3E,4A,5D
1E,2D,3A,4C,5B
1
4,5
3
3,4
1E,2B,3A,4D,5C
11
12
13
14
15
16
17
18
19
20
3
2,3
1,3
3
1,2,5
2,3,4
5
1,2,4
3,5
2
31
32
33
34
35
36
37
38
39
40
4
2,4,5
2
1,2,3
3
1,2
1D,2C,3A,4E,5B
1,4
1A,2B,3E,4C,5D
5
51
52
53
54
55
56
57
58
59
60
1,2
2,3
1A,2B
2
1E,2D,3B,4C,5A
2,4
1,2,5
5C
1D,2A,3B,4C
2
Creator of the programme _______________________ Kuznetsova O.M.
Director of the programme
______________________ Chernov N. N.