
- •Section I Control of the initial level of knowledge. Biochemical constituents of the cell. Methods of biochemical investigations.
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •77. Discribe the method, shown at the picture below:
- •78. Discribe the method, shown at the picture below:
- •Section іі Enzymes, structure and classification. Regulation of metabolism
- •Е. Whatever part of polypeptide chain of enzyme molecule.
- •Substrate concentration at which reaction rate is half maximal
- •The second enzyme has higher affinity to substrate
- •Competitive
- •Examples of Krok 1 tests
- •Cysteine
- •B. Amylase
- •Peptidases
- •Enteropeptidase
- •Clinical cases and Situational tasks
- •Section ііi Metabolic pathways and bioenergetics. Tricarboxylic acid cycle. Biological oxidation and oxidative phopshorylation
- •1. When atp forms amp:
- •B. Protons
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section іv Structure and metabolism of carbohydrates
- •19. Chose the reaction of glycolysis catalyzed by an enzyme phosphofructokinase:
- •A. Liver
- •Examples of Krok 1 tests
- •Acetoacetate, β-hydroxybulyrate, and acetone
- •Clinical cases and Situational tasks
- •Section іv Structure and metabolism of lipids
- •Examples of Krok 1 tests
- •143. A patient with high rate of obesity was advised to use carnitine as a food additive in order to enhance "fat burning". What is the role of carnitine in the process of fat oxidation?
- •144. Lipids are obvious energetic material for the body. What is the main pathway of fatty acids metabolism in mitochondria?
- •Clinical cases and Situational tasks Situational tasks
- •179. The patient is observed an allocation of undigested fat in the faeces. What are the possible causes for this?
- •184. Free cholesterol can affect cholesterol metabolism in the body by inhibiting cholesterol biosynthesis. By which step free cholesterol can inhibit its biosynthesis?
- •186. Explain the mechanism of phospholipids breakdown, shown at the scheme below:
- •Section VI Structure and metabolism of amino acids
- •B. Amylase
- •Examples of Krok 1 tests
- •112. According to clinical indications a patient was administered pyridoxal phosphate. What processes is this medication intended to correct?
- •Clinical cases and Situational tasks
- •145. In a patient 10 g of urine per day is excreted. Evaluate this result.
- •151. Skin color is the aggregate result of the expression of a number of genes modified by ethnic origin and genetic inheritance. What can cause the hypopigmentation?
- •Section VII Principles of molecular biology and molecular genetics
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •108. List and describe properties of the genetic code.
- •113. Fill in the blanks.
- •114. Put the numbers of the enzymes on their place in the picture. Using arrows indicate the direction of replication and direction of synthesis of leading and lagging strands.
- •Section VIII Molecular mechanisms of hormone action on target cells. Biochemistry of hormonal regulation
- •Examples of Krok 1 tests
- •78. For analgesia, a certain substance which imitates the physiological properties of morphine but is synthesized inside the human brain can be used. Name this substance.
- •80. A patient suffering from rheumatism was administered glucocorticoid therapy. What changes in carbohydrate metabolism in liver can be expected?
- •88. In blood of a patient a hypercalcemia, hypophosphatemia, in urine – hyperphosphaturia is observed. What is a possible cause of this state?
- •90. In 13 years old girl a hypotension and polyuria is observed. Preliminary diagnosis – diabetes insipidus. It is caused by deficiency of:
- •93. Signaling via prostanoids begins by interaction of the prostanoid with its receptor. The receptor involved is usually located in which part of the cell?
- •Clinical cases and Situational tasks
- •97. In 13 years old girl a hypotension and polyuria is observed. Preliminary diagnosis – diabetes insipidus. Which hormone deficiency can cause this disease?
- •99. The thyroid hormones t3 and t4 are synthesized in the follicular cells of the thyroid gland. From which of the following essential amino acids are the thyroid hormones synthesized?
- •101. Name types of signalling:
- •Section IX Biochemistry of the nervous tissue
- •С. Ketone bodies
- •24. What compound may be used by the cns cells after extensive physical exercises and prolonged starvation?
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •114. Describe the structure of a synapse and explain how it operates?
- •Section X Biochemistry of the Muscular tissue
- •D. Glycogenolysis in muscles
- •С. Fatigue faster compared to the red fibers
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section XI Biochemistry of nutrition
- •1. Note substance, which activates pepsinogen to pepsin:
- •2. Chose the enzyme which plays an important role in production of hydrochloric acid by parietal cells of gastric mucosa glands:
- •3. Which of the following is not a function of the pancreas?
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •62. The clinical and laboratory examination of the patient evaluated the presence of the lactic acid in his gastric juice. What does it indicate? What should be recommended to the patient?
- •69. Discribe the mechanism of hydrochloric acid production shown at the picture:
- •Section XII Functional role of water soluble and fat soluble vitamins in metabolism and providement of cell functions
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •100. A deficiency in thiamine (vitamin b1) would most likely lead to which clinical manifestations?
- •Section XIII Biochemistry and pathobiochemistry of blood
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •89. The blood clotting cascade in humans is represented in the picture below. Using this scheme answer the following questions:
- •Section XIV Functional and clinical biochemistry of liver tissue. Biotransformation of xenobiotics and endogenous toxic compounds
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section XV Water and mineral metabolism
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section XVI Functional role of kidneys in urinogenesis. Normal and pathological constituents of urine
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section XVII Biochemical constituents of connective tissue
- •Examples of Krok 1 Tests
- •Clinical cases and Situational tasks
- •34. Patient with burn disease is at the risk of formation of blood clots in blood vessels. What glycosaminoglycan may be used to prevent formation of blood clots?
- •Section XVIII Biochemistry of saliva and tooth tissue
- •Examples of Krok 1 tests
- •Clinical cases and Situational tasks
- •Section XIX. Biochemical reactions
- •References:
Е. Whatever part of polypeptide chain of enzyme molecule.
10. As cofactors of enzymes the most frequently met are the next compounds:
A. Vitamins, modified by cell enzymes (vitamin derivatives)
B. Native vitamins
C. Hormons, e.g.thyroxine
D. Carbohydrates
E. Polynucleotides
11. Nonprotein part of complex (conjugated) enzyme is called as:
A. Coenzyme
B. Holoenzyme
C. Apoenzyme
D. Allosteric activator
E. Allosteric suppressor
12. Chose the correct statement about allosteric site of enzyme:
It modulates reversibly enzymatic activity after binding with ligand
It is identical with active center
It serves for attachment of enzyme to biomembrane
It irreversibly inhibits enzymatic activity after binding with ligand
It induces chemical modification of enzyme molecule
13. The active site of an enzyme is formed by:
R group of amino acids
NH2 group of amino acids
CO group of amino acids
Sulphur bonds which are exposed
Peptide bonds
14. Coenzymes are:
Heat stable, dialyzable, non protein organic molecules
Soluble, colloidal, protein molecules
Structural analogue of enzymes
Different forms of enzymes
Inorganic catalists
Allosteric suppressor
15. Coenzymes combine with:
Apoenzymes
Proenzymes
Holoenzymes
Antienzymes
Cofactors
16. Active centers in nonconjugated (simple) enzymes, e.g.trypsin, are formed by the next constituents of enzyme molecule:
Amino acid side chains only
Peptide bonds between selected amino acids
Nucleotides
Carbohydrates
Phospholipids
17. Chose the amino acid, which is frequently involved in formation of active center in different enzymes.
Histidine
Leucine
Proline
Valine
Glycine
18. Which from the listed below is coenzyme?
All of these
ATP
Vitamins B and C
CoQ and CoA
Thiamine
19. How are called enzymes which catalyze the same reaction, are of the same origin but differ in chemical properties?
Izoenzymes
Apoenzyme
Coenzyme
Holoenzyme
Zymogen
20. Multiple forms of the same enzymes are known as:
Isoenzymes
Zymogens
Proenzymes
Pre-enzymes
Coenzymes
21. Enzymes activity is controlled by
All of these
pH of the solution
Temperature
Concentration of the enzyme
Concentration of the substrate
22. Boiling destroys the activity of enzyme irreversibly due to the next process:
Change in conformation of enzyme molecule
Cleavage of peptide bonds in polypeptide chain of enzyme.
Cleavage of disulphide bonds in enzyme molecule
Cleavage of ionic bonds in enzyme molecule
Formation of intramolecular or intermolecular cross-links in enzyme molecule
23. In humans most enzymes have an optimal temperature of action at:
37 oC
0 oC
20 oC
30 oC
100 oC
24. What happens with enzymes at 90 oC?
Denaturation
Hydrolysis
Alteration of primary structure
Alteration of tertiary structure
Tight binding of substrate in active site
25. The pH optima of most of the enzymes is:
Between 6 and 8
Between 1 and 3
Between 4 and 6
Between 8 and 12
Above 12
26. Pepsin has the next pH optimum for enzymatic activity:
pH 1,5
pH 5,1
pH 7,5
pH 8,0
pH is non significant
27. Trypsin exhibits maximal catalytic activity at the next pH value:
A. pH 7,5
B. pH 5,1
C. pH 2,5
D. pH 9,5
E. pH is non significant
28. Chose from listed below enzymes, ONE which represents class hydrolases:
Pepsin
Aldolase
Glucokinase
Phenol oxidase
ATP synthase
29. Enzymes, providing polysaccharide hydrolysis are defined as:
Glycosidases
Lipase
Phosphatase
Catalase
Proteases
30. The first position in classification of enzymes is occupied by:
Oxidoreductases
Transferases
Isomerases
Hydrolases
Ligases
31. The fourth position in classification of enzymes is occupied by:
Lyases
Transferases
Isomerases
Hydrolases
Ligases
32. The code number of each individual and well characterized enzyme contains the next ranges of figures:
Four
Two
Three
Five
Six
33. Chose from list below enzymes, which exhibits specificity to peptide bonds:
Chymotrypsin
Urease
Alcohol dehydrogenase
Arginase
Cellulase
34. What type of reactions presented below is catalyzed by hydrolases?
A-B + H2O = A-OH + B-H
AH2 + B = A + BH2
A+B+ATP= A-B + ADP + Pi
A-B = A + B
A-R-B = A-B-R
35. What type of presented below reactions is catalyzed by dehydrogenases?
AH2 + B = A + BH2
A+B+ATP= A-B + ADP + Pi
A-B + H2O = A-OH + B-H
A-B = A + B
A-R-B = A-B-R
36. The best example of extracellular enzymes (exoenzyme) is:
Digestive enzymes
Nucleases
Succinic dehydrogenase
Malatedehydrogenase
None of these
37. The substrate for amylase is:
Starch
Cane sugar
Lactose
Ribose
Maltose
38. In cell, digestive enzymes are found mainly in:
Lyzosomes
Mitochondria
Ribosomes
Nucleus
Vacuoles
39. A mitochondrial marker enzyme is:
Succinate dehydrogenase
Aldolase
Amylase
Pyruvate dehydrogenase
DNA-polymerase
40. The third position in classification of enzymes is occupied by:
A. Hydrolases
B. Transferases
C. Lyases
D. Isomerases
E. Ligases
41. In human saliva there is an enzyme able to hydrolyze the α[1→4] glucosidic bonds in the molecule of starch. Name this enzyme:
α-Amylase
Phosphatase
Fructofuranosidase
β-Galactosidase
Lysozyme
42. In the cell, enzymes are located in subsequent organelles, providing their specific functioning. Note enzymes located in lysosomes.
Cathepsins and glucosaminidase
Fatty acid synthesis enzyme complex
Enzymes of protein biosynthesis
Enzymes of urea synthesis
Glycogen synthetase and branching enzyme
43. Cytochrome c participates in transport of electrons in respiratory chain of the cell and is located in the next cellular compartment:
Mitochondria
Nucleus
Cytoplasm
Golgi vesicles
Lysosomes
44. In a patient was detected disorder in digestion of protein in stomach and small intestines. What group of enzymes may cause this disorder?
А. Proteinases
В. Amylase
С. Lipase
D. Lyases
Е. Aminotransferases
45. Chose from list below enzymes located in nucleus:
RNA polymerases
Enzymes of protein biosynthesis
Enzymes of tricarboxylic acid cycle
Cathepsins and glucosaminidase
Glycogen synthetase and branching enzyme
46. The enzymes of the citric acid cycle are located in:
Mitochondrial matrix
Extramitochondrial soluble fraction of the cell
Nucleus
Endoplasmic reticulum
Lysosomes
47. Chose from list below, enzyme belonging to class of hydrolases:
Thrombin
Lactate dehydrogenase
Glucokinase
Phenol oxidase
Aldolase
48. Chose from listed below enzymes, ONE which exhibits specificity to peptide bonds:
A. Chymotrypsin
B. Urease
C. Alcohol dehydrogenase
D. Arginase
E. Cellulase
49. Activity of multienzyme complexes is regulated by the next type of regulation:
Feedback inhibition
Catabolic repression
Limited proteolysis
Non competitive inhibition
Competitive inhibition
50. Proenzymes:
All of these
Chymotrysinogen
Pepsinogen
Proelastase
Trysinogen
51. An allosteric modulator influences enzyme activity by:
Binding to a site on the enzyme molecule distinct from the catalytic site
Competing for the catalytic site with the substrate
Changing the nature of the product formed
Changing the specificity of the enzyme for its substrate
Covalent modification of enzyme
52. In active center of enzymes which catalyze hydrolysis of substrate (hydrolases) usually is present the next amino acid residue:
Histidine
Leucine
Phenylalanine
Proline
Valine
53. In active center of enzyme very frequently is present side chain of the next amino acid:
Histidine
Leucine
Phenylalanine
Proline
Valine
54. Activity of many enzymes depends from the presence of free thiol groups in active center. What amino acid residue provides presence of these groups in enzyme molecule?
Cysteine
Lysine
Tryptophan
Methionine
Serine
55. Michaelis-Menten constant (Km) reflects the next property of enzyme:
Affinity to substrate
Thermolability
Sensitivity to pH of medium
Affinity to a product of reaction
Sensitivity to competitive inhibitors
56. Michaelis-Menten constant corresponds to: