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100. A deficiency in thiamine (vitamin b1) would most likely lead to which clinical manifestations?

Answer: In addition to being an important cofactor for the enzymes involved in the oxidative decarboxylation of pyruvate, α-ketoglutarate, and branched-chain α-ketoacids, thiamine is also a cofactor for the enzyme transketolase, the enzyme that transfers a glycoaldehyde group from a ketose sugar to an aldose sugar in the pentose phosphate pathway. One of the diagnostic tools in determining a thiamine deficiency is determination of the activity of red blood cell transketolase in the presence and absence of added thiamine. A thiamine deficiency would be expected to increase blood lactate concentrations. A deficiency of biotin would lead to decreased carboxylase activity, whereas an increased methylmalonate concentration would be observed with a deficiency in vitamin B12. A deficiency in vitamin K would lead to an increase in prothrombin time.

101. Name types of vitamin B6 shown at the picture:

1 2 3

Answer: 1 – pyridoxine, 2 – piridoxal, 3 – piridoxamine.

Section XIII Biochemistry and pathobiochemistry of blood

1. Fibrinogen is transformed into fibrin monomer by the next biochemical process:

  1. Limited proteolytic cleavage

  2. Phosphorylation with involvement of ATP and proteinkinase

  3. Dephosphorylation by protein phosphatase

  4. Carboxylation of glutamic acid residues

  5. Acetylation with involvement of acetyl-CoA.

2. For extrinsic pathway of blood coagulation the next factor is necessary:

  1. Proconvertin (VII)

  2. Hageman factor (XII)

  3. Christmas factor (IX)

  4. Kallicreine

  5. Plasma thromboplastine antecedent (XI)

3. Light chains of immunoglobulins are of following types:

  1. Kappa and lambda

  2. Alpha and kappa

  3. Alpha and gamma

  4. Lambda and delta

  5. Alpha and beta

4. Prothrombin is activated and transformed to thrombin by an active form of the next intrinsic factor:

  1. Plasma thromboplastin antecedent (X)

  2. Convertin (factor VII)

  3. Antihemophilic globulin A (VIII)

  4. Hageman factor (XII)

  5. Christmas factor (IX)

5. Hemophilia A is caused by deficiency of the next blood coagulation factor:

  1. Antihemophilic globulin A

  2. Proconvertin

  3. Proaccelerin

  4. Tissue thromboplastin

  5. Christmas factor

6. Immunoglobulins are classified on the basis of:

  1. Type of heavy chains

  2. Type of light chains

  3. Types of light and heavy chains

  4. Molecular weight

7. Post translational modification of coagulation factors and formation of γ-carboxyglutamic acid has the next functional significance:

    1. Increases the affinity to Ca ions

    2. Decreases the affinity to Ca ions

    3. Induces formation of additional ionic bonds in peptide chain

    4. Induces appearance of Mg ion ligands in protein molecule

    5. Provides cross linking of fibrin filaments

8. The molecular weight of heavy chains of immunoglobulins is:

  1. 50,000–70,000 Da

  2. 20,000–25,000 Da

  3. 25,000–50,000 Da

  4. 70,000–1,00,000 Da

  5. 1,00,000-5,00,000 Da

9. Thrombin belongs to the next class of enzymes:

  1. Hydrolases

  2. Oxido-reductases

  3. Transferases

  4. Lyases

  5. Isomerases

  6. Ligases

10. Plasminogen is activated and transformed to the active form plasmin by the following enzyme:

  1. Urokinase

  2. Thrombin

  3. Thrombokinase

  4. FSF (fibrin stabilization factor)

  5. Ca ions

11. The most abundant immunoglobulin in plasma is:

  1. IgG

  2. IgA

  3. IgM

  4. IgD

  5. IgE

12. Allergic reactions are mediated by:

  1. IgE

  2. IgA

  3. IgG

  4. IgD

  5. IgM

13. C1 component of classical complement pathway is made up of:

  1. Complements 1q and 1r

  2. Complements 1q and 1s

  3. Complements 1r and 1s

  4. Complements 1q, 1r and 1s

14. Which from listed below immunoglobulins is secretoty and inhibits adsorption and growth of bacteria on mucosa surfaces?

A.IgA

B. IgM

C. IgD

D. IgE

E. IgG

15. IgG cleaved by papain into:

  1. Two Fab and one Fc fragments

  2. Two light and two heavy chains

  3. Two pairs of one light and one heavy chain each

  4. One Fab and two Fc fragments

16. Severe combined immunodeficiency (SCID) is caused by congenital defect of the next enzyme:

  1. Adenosine deaminase

  2. Alanyl aminotransferase

  3. Transketolase

  4. Adenosine phosphorylase

  5. AMP nucleotidase

17. Chose the symbol of heavy chain type in immunoglobulin M:

A. μ

B. β

C. γ

D. λ

E. α

18. Immunoglobulin M molecule possesses the next quaternary structure:

A. It is pentameric molecule

B. It is dimeric molecule

C. It is trimeric molecule

D. It is tetrameric molecule

E. It is monomeric molecule

19. The antibody class which can pass through the placenta to protect the fetus is

A. Immunoglobulin G (IgG)

B. Immunoglobulin M (IgM)

C. Immunoglobulin A (IgA)

D.Immunoglobulin D (IgD)

E.Immunoglobulin E (IgE)

20. The minimum number of polypeptide chains in an immunoglobulin is:

  1. Four

  2. Two

  3. Five

  4. Six

  5. Seven

21. Cross linking of fibrin monomers in the filament and formation of tight clot is provided by the next factor:

      1. FSF (fibrin stabilization factor)

      2. Plasmin

      3. Thromboplastin

      4. Convertin

      5. Accelerin

22. Chose from listed below factors one of the extrinsic pathway of blood coagulation:

  1. Proconvertin

  2. Prothrombine

  3. Antihemophilic globulin A

  4. Hageman factor

  5. Proaccelerin

23. Chose from presented vitamins one with antihemorrhagic activity:

A. Philloquinone

B. Retinol

C. Tocopherol

D. Ergocalciferol

E. Pangamic acid

24. Vitamin K serves as a cofactor in the next enzymatic reaction:

A. Carboxylation of glutamic acid side chain

B. Decarboxylation of glutamic or aspartic acid side chain

C. Limited proteolytic cleavage of zymogens

D. Phosphorylation of serine or threonine

E. Amidation of glutamic acid side chain

25. The molecular weight of light chains of immunoglobulins is:

  1. 20,000–25,000

  2. 10,000–15,000 Da

  3. 25,000–50,000 Da

  4. 50,000–75,000 Da

  5. 75,000-100,000 Da

26. Secretory component is present in:

  1. IgA

  2. IgG

  3. IgM

  4. IgD

  5. IgE

27. The components of complement system are activated by:

  1. Phosphorylation

  2. Microsomal hydroxylation

  3. Glycosylation

  4. Proteloysis

28. Chose the symbol of light chain type of immunoglobulins:

  1. λ

  2. α

  3. β

  4. γ

  5. μ

29. Hemophilia B is caused by deficiency of the next blood coagulation factor:

A. Christmas factor (factor IX)

B. Proaccelerin

C. Antihemophilic globulin A

D. Tissue thromboplastin

E. Proconvertin

30. Chose the correct value of normal protein concentration in human blood plasma:

A.65-85 g/l

B.45-60 g/l

C.25-40 g/l

D.85-100 g/l

E.100-150 g/l

31. Proteins of blood plasma are divided into albumin and globulins. What is quantitative proportion of albumin to globulins (albumin/globulin coefficient)?

A.1.5:2

B.2:1

C.5:1

D.1:1

E.1:5

32. The three primary types of plasma proteins are:

  1. Albumins, globulins, fibrinogen

  2. Heme, iron, globin

  3. Antibodies, metallo-proteins, lipoproteins

  4. Serum, fibrin, fibrinogen

  5. None of the above

33. The predominant constituent of blood rest nitrogen is:

A. Urea

B. Creatinine

C. Bilirubin

D. Phenylalanine

E. Glutathion

34. One of the components of blood residual nitrogen fraction is bilirubin, which is produced from:

A. Heme

B. Cholesterol

C. Levulinic acid

D. Creatinine

E. Tryptophan

35. Uric acid is a final product of catabolism of the next component of nucleic acids

A. Guanine

B.Phosphate

C.Thymine

D. Ribose

E. Orotat

36. Myoglobin belongs to:

A. Hemoproteins

B. Albumins

C. Glycoproteins

D. Transferrins

E. Phosphoproteins

37. Hemoglobin belongs to?

A. Chromoproteins

B. Nukleoproteins

C. Phosphoproteins

D. Lipoprotein

E. Glycoproteins

38. The structure of heme in hemoglobin is:

A. Protoporphyrin IX, attached to the Fe2+

B. Four pyrrol rings, attached to Fe3+

C. Four pyrrol rings, attached to Fe 2+

D. Porphyrin coupled with Fe

E. Protoporphyrin X, attached to and Fe 3+

39. Protoporphyrin IX belongs to one of the following:

A. Hemoglobins

B. Transferrins

C. Ceruloplasmins

D. Properdins

E. Cryoglobulines

40. Methylene blue promotes oxidation of hemoglobin. Give the name of the obtained compound:

A. Methemoglobin

B. Hematin

C. Hemine

D. Carboxyhemoglobin

E. Carbhemoglobin

41. Thalassemia is a genetic disorder of synthesis of one of the chains of hemoglobin. Inhibition of β - chain synthesis leads to formation of β-thalassemia. Which of the following will be the best feature of the disease?

A. Increased concentration of hemoglobin F

B. Decreased concentration of hemoglobin F

C. Hemolytic anemia.

D. Sickle erythrocyte shape

E. Reduction of hemoglobin A2

42. In complex proteins their prosthetic group is associated with protein moiety. Choose from the list one amino acid responsible for the formation of bonds between these two parts:

A. Histidine

B. Serine

C. Alanine

D. Tyrosine

E. Lysine

43. Choose from the following a major end product of protein metabolism that is excreted in the largest quantity of urine:

A. Ammonia and ammonium salts

B. Glutamine

S. Uric acid

D. Allantoin

E. Urea

44. What from the following belongs to nitrogen-free organic compounds?

A. Vitamin C

B. ATP

C. Glucagon

D. Glutamine

45. What physical and chemical properties of blood explain the presence of electrolytes?

A. Osmotic pressure

B. Oncotic pressure

C. Erythrocyte sedimentation rate

D. Viscosity of blood

46. In erythrocytes carbonic acid is formed from CO2 and H2O. What enzyme provides a synthesis of carbonic acid in erythrocytes and its degradation in the capillaries?

A. Anhydrase

B. Amylase

C. Elastase

D. Alkaline phosphatase

E. Lipase

47. Hemoglobin differs from similar proteins by specific physical and chemical properties. Indicate physical and chemical properties that distinguish hemoglobin from myoglobin?

A. Molecular weight

B. Solubility

C. Electrophoretic activity

D. Spectral properties

48. As a complex protein, hemoglobin consists of protein and non-protein moieties. Indicate the components of hemoglobin.

A. 4 Hem groups, 2 α - and 2 β - polypeptide chains

B. Hem, 1 α - and 3 β - polypeptide chains

C. 4 Hem groups and 4 β - polypeptide chains

D. 4 Hem groups and 4 α -polypeptide chains

E. Hem, 2 α - and 2 β - polypeptide chains

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