1. Description discipline Biochemistry of Animals with the Fundamentals of Fhysical and Colloidal Chemistry, р.2
(name)
Field of knowledge, direction of training, specialty, education and qualification level
Educational Degree «Bachelor» Direction of training «Veterinary Medicine» Specialty 211 - «Veterinary Medicine»
Specialization
Characteristics of discipline
Kind Regulatory
Total hours 75
Number of ECTS credits 2,5
Number of thematic modules 3
Course project (work) (if it is in the working educational plan)
-
Form of control an examination
Indicators discipline for full-time and extramural study
full-time study extramural study
Year of training 2
Semester 3
Lectures 30 hours.
Practical classes, seminars - hours.
Laboratory classes 30 hours
Self-work 15 hours.
Self-work under supervising tutor - hours.
Number of weekly hours
for full-time study:
classroom
self-work of student −
5 hours.
1. The purpose and tasks discipline
The purpose of "Biochemistry of Animals with the Fundamentals of Physical and
Colloidal Chemistry" is to equip students by complete system of knowledge about the
chemical composition of living organisms, physico-chemical and biological properties
of natural compounds, the main pathways of metabolism, regulatory mechanisms and
the relationship of metabolic processes that is to take on theoretical fundamentals of
metabolic transformations and their regulation in animals and practical skills of their
study.
Tasks of the course "Biochemistry of Animals with the Fundamentals of Physical
and Colloidal Chemistry" are to learn the basics of life organisms, namely: structure,
physico-chemical and biological properties of substances and their metabolism and its
regulation and metabolic changes using as feed and as medicines to promote health and
improve animal productivity.
After study of the discipline, the student must
know: - chemical fundamentals of life organisms, including chemical structure and
properties of natural compounds and their complexes, major pathways and mechanisms
of regulation of metabolism, biochemical mechanisms of realization of genetic
information;
- theoretical and practical importance of biochemistry and its relationship with
other natural sciences;
- the latest achievements of biochemistry and prospects for their use in various
sectors of the national economy, especially in veterinary medicine;
be able: to orientate in biochemical studies at the present level, namely: to choose the
appropriate physico-chemical and biochemical methods and methodological approaches
and equipment, select biological samples, possess conventional methods of
determination in biological objects of various metabolites, indexes with devices
biochemical laboratory for characteristics of the physiological state of animals, and its
changes.
2. The program and structure of study discipline:
– full-time study
Thematic Module 1. Regulatory effects of inorganic and organic substances on the
metabolism
Theme of lecture lesson 1. Water and mineral balance and its effect on the
metabolism
Subject and tasks of biochemistry. Contribution of the Ukrainian biochemists to the
development of biochemistry. Water, its exchange and state in the organism. Sorption.
Regulation. Abnormal states of water’s exchange.
Quantity elements (macroelements) and essential trace elements (microelements).
Biochemical functions of inorganic substances.
*Electrolyte balance of organisms. Regulation and abnormal states of mineral
turnover (*it’s pointed themes of self-work in the thematic material of lectures).
Theme of lecture lesson 2. Vitamins. Coenzymes
Regulators of metabolism: vitamins. Common characteristcs. Vitaminology. Fat-
soluble vitamins: A and D with their vitamers, E, K, and F. Water-soluble vitamins: for
example, В1 (thiamine); В2 (riboflavin); В3 (pantothenic acid); В5 (nicotin amide або
vitamin РР); В6 (pyridoxal, pyridoxine, pyridoxamine or vitamin B6); В7or8 (Н or biotin);
В9 (Вс or folic acid), В12 (cyanocobalamin).
*Precursors of vitamins (carotinoides - precursor of vitamin А). Sources of
vitamins. Vitamin-like substances: inositol; vitamin В4 (choline); vitamin В11, (Вт,
carnitine); vitamin В13 (orotic acid); vitamin В15 (пангамова acid); p-aminobensoic
acid (PABA). Antivitamins. Avitaminosis, hypo- and hypervitaminosis of farm animals.
Coenzymes (thiamine diphosphate, FAD, FMN, Coenzym А, NAD, NADP,
pyridoxal phosphate, biocytin, lipoamides, 5’-deoxyadenosylcobalamin, methyl
cobalamin) and their role in catalytic processes under action of enzymes.
Theme of lecture lesson 3. Enzymes and their kinetic properties
Common information concerning enzymes: structure, definition of substrate,
active center, enzyme-substrate complex, substrate specificity. Cofactors and
coenzymes. Equation of enzymatic reaction. Mechanism of enzymatic reaction with one
substrate. Enzyme numbers and their classification. The enzyme classes: 1) oxido-
reductase, 2) transferase, 30 hydrolase, 4) lyase, 5) isomerase, 6) ligase, and typical
reactions for enzymes of each class.
*The terms those are used in enzymology. Enzyme kinetics. Influence of physical
and chemical factors on enzymatic activity. Activators and inhibitors of enzymes.
Theme of lecture lesson 4. Hormones and mechanisms of their influence on
metabolic processes
Regulators of metabolism: hormones. General characteristics.
*Structure of molecules, biosynthesis, metabolism. Types of communication
between cells (direct contact, neurotransmitters, and endocrine signaling molecules).
Depending on the speed of the signals those are distinguished on the following types of
signaling: for neurotransmitters, it occurs and is extinguished in milliseconds signal,
the receptor proteins which are ion channels postsynaptic membrane; for protein and
peptide nature hormones, catecholamines, prostaglandins, signal transmission takes
minutes and its receptors located on the plasma membrane; for steroid and thyroid
hormone, signaling occurs over hours, days and they are perceived receptors in the
cytosol and nucleus.
Mechanisms of hormonal influence on metabolic processes.
Thematic Module 2. Biochemistry: Dynamics
Theme of lecture lesson 1. Biochemistry of digestion and features of digestive
processes in different organisms
Biochemistry of digestion. Cavity, parietal, membrane, cellular digestion.
Biological features of absorption of substances. Features of protein digestion in
ruminants, transformation of Nitrogen-containing non-protein substances. Digestive
hormones (gastrin, secretin, cholecystokinin, gastric inhibitor peptide and motylin). The
formation of hydrochloric acid. Transmembrane transport of substances: simple
diffusion, passive transport (facilitated and exchange diffusion), active transport
(primary and secondary transport) endocytosis and exocytosis. Two types of
endocytosis: phagocytosis and pinocytosis.
*Mechanisms of transport. Digestion of nutrients (proteins, carbohydrates,
nucleic acids, lipids, vitamins and inorganic substances, cellulose), enzyme hydrolysis
(hydrolysis products: amino acids, monosaccharides, nitrogenous bases, pentose,
phosphate, nucloeside, 2-monoacyl glycerol, FA, cholesterol, cellulose, lignin), re-
sorbtion (hydrophilic and lipophilic substances), or transport through the blood to the
liver, portal vein, lymphatic system. Digestive enzymes of proteins, carbohydrates,
nucleic acids, lipids.
Theme of lecture lesson 2. Metabolism of carbohydrates and its peculiarities (in
ruminants) (1)
Carbohydrate metabolism. Intermediary carbohydrate metabolism in the organs
and tissues. Anaerobic decomposition of carbohydrates - glycolysis (its stages,
reversible and irreversible reactions and regulation), glycogenolysis. Regulatory
enzymes of glycolysis.
*Pasteur Effect (inhibition of glycolysis reactions in conditions of activation of
cellular respiration). The value of anaerobic glycolysis.
The pathways of glucose transformation. Glucose-lactate cycle (cycle Corey).
Metabolic conversion of glucose-6-phosphate in erythrocytes. Glycolysis and
glycogenolysis in different states of the organism and the ways of their correction.
Hypo-and hyperglycemia.
Theme of lecture lesson 2. Metabolism of carbohydrates and its peculiarities (in
ruminants) (2)
Peculiarities of carbohydrate metabolism in ruminants. Pentose phosphate
(phosphogluconate) pathway (PPP): its stages and their functioning (including
erythrocytes). The biological significance of PPP. Hereditary deficiency of glucose-6-
phosphate dehydrogenase (enzyme PPP) causing hemolysis of erythrocytes.
Synthesis of glucose, glycogen, lactose.
Gluconeogenesis, characterization bypass reactions of glycolysis and its hormonal
regulation (including insulin, glucagon, epinephrine and glucocorticoids). Glucose-
lactate cycle (cycle Corey). Glucose-alanine cycle.
Propionate (product of carbohydrate metabolism by microorganisms) - the main
substrate of gluconeogenesis in ruminants.
*Glucogenous amino acids. Cooperation between glycolysis and
gluconeogenesis.
Effect of antagonistic hormones (insulin and glucagon) and hormone-synergists
(glucagon, epinephrine, corticosteroids, somatropin) on carbohydrate metabolism.
*Glycogenesis, synthesis of lactose in the lactating mammary gland and non-
lactating tissues.
Theme of lecture lesson 3. Amphibolic transformation of organic substances (the
tricarboxylic acids cycle). Energy of biochemical processes
The tricarboxylic acids cycle (TCAC or citric acid cycle, or Krebs’ cycle) TCAC:
enzymes and sequence of reactions. Reduction of NAD and FAD, phosphorylation on
the level of substrate. Energy balance of TCAC. Usage of metabolities of TCAC in
metabolism of carbohydrates, lipids, amino acids, proteins, nucleic acids and their
components (common characteristics).
Biological oxidation , types of biological oxidation.
*The modern theory of tissue respiration. The theory of oxidative
phosphorylation. Main macroergic compounds. Oxidation coupled with
phosphorylation of ADP (substrate and oxidative phosphorylation). Principles of
structural and functional organization of electron transport (respiratory) chain of
mitochondria. NAD-and NADP-dependent dehydrogenase flavin enzymes, ubiquinone,
cytochromes and cytochrome oxidase. Mechanisms of coupling of oxidation and
phosphorylation in the respiratory chain.
Transmembrane potential of protons, ATP synthase work.
Theme of lecture lesson 4. Metabolism of lipids (1)
Exchange of lipids. Lipid digestion and absorption of the products of their
hydrolysis. Role of bile acid in digestion of lipids. Intermediate lipid metabolism in the
organs and tissues. Transportation forms of lipids (lipoprotein complexes) functions
apo-proteins. Lipolysis (catabolism) of TAG. The molecular basis for the regulation of
adipocyte triacyl glycerol lipase activity - its covalent modification by reversible
phosphorylation-dephosphorylation.
*Adenilate cyclase mechanism for the regulation of lipolysis. Hormonal
regulation of lipolysis. Catabolism of phospholipids sterides. Ketonogenesis (formation
of ketone bodies: acetone, aceto acetate, beta-hydroxybutyrate). Reactions of utilization
of ketone bodies. Metabolism of ketone bodies in pathological conditions.
Theme of lecture lesson 4. Metabolism of lipids (2)
Exchange of glycerol and fatty acids (FA). β-oxidation of FA (sequence of
reactions and their localization) and its energy. Oxidation of unsaturated fatty acids.
Oxidation FA with an odd number of carbon atoms. β-oxidation FA (C20 and more than
20 carbon in the Carbon-chain of FA). α-and ω-oxidation of FA. Cleavage of branched
of FA during α-oxidation. ω oxidation (as detoxification of intermediates of defective β-
oxidation) in the smooth endoplasmic reticulum of liver. Oxidation of glycerol and its
energy. Coordinated regulation of metabolism of FA. Synthesis of FA (role
multienzyme complex).
*Elongation of the saturated FA. Formation of the unsaturated FA. Metabolic
pathways of biosynthesis of saturated and unsaturated FA by enzyme systems in the
organism. The formation of glycerol. Lipogenesis is the synthesis of neutral fats
(triacylglycerols, TAG). Ways of TAG synthesis and phospholipids.
Theme of lecture lesson 5. The metabolic processes of proteins and some amino
acids (1)
Biochemistry of proteins. Proteins complete and defective on essential amino
acids. The biological value of proteins. Essential amino acids. Exchange of some amino
acids. Absorption of amino acids. Digestion of proteins. Enzymes of digestion of
proteins. Proteolysis and proteolytic enzymes. Predecessors of proteolytic enzymes
(trypsinogen, himotrypsynohen, proelastase). Intracellular proteolysis of proteins in
lysosomes. Degradation of proteins in proteasome which is localized in the cytoplasm.
*Proteins decay in colon and disposal processes of generated toxic products. The
formation of the end products of protein metabolism (H2O, CO2, NH3). Ways of removal
of ammonia. Ornithine cycle of formation of urea. Abnormality of the urea cycle
formation cause disorders such as argininemia.
Common ways of converting amino acids. Reactions of conversion of amino
acids: deamination, decarboxylation, transamination of amino acids (aspartate
aminotransferase or AST and alaninaminotransferase or ALT). Biochemical value of
conversion of amino acids.
Protein synthesis. Synthesis of somel amino acids, peptides (insulin, glucagon,
glutathione) and protein. Nitrogen balance in the body is primarily determined by the
metabolism of protein. Protein biosynthesis (translation) and its stages (initiation,
elongation, termination). Translation in prokaryotes and eukaryotes. Effect of antibiotics
on the process of protein synthesis. Synthesis of insulin. Effect of insulin on glucose
uptake by the cell and on metabolism glucose. Synthesis of glutathione and its
antioxidant role.
*Synthesis of amino acids through transamination reactions: pyruvate (glycolytic
end product) -> alanine; oxaloacetate (intermediate of TCAC) -> aspartate, alpha-
ketoglutarate (intermediate of TCAC) -> glutamate. Synthesis of glycine and role of
tetrahidrofolate.
Theme of lecture lesson 6. Catabolism and anabolism of nucleotides and nucleic
acids (1)
Catabolic processes of nucleic acids (NC). Exchange of nucleic acids.
Nucleoprotein digestion, absorption of hydrolysis products. Effect of antibiotics on
nucleoproteins. Enzymes hydrolysis of NA (endonuclease and exonuclease). The
specificity of nucleases: RNase, DNAase, non-specific nucleases. 3'-and 5'-nuclease.
The decay of NA in tissues. Catabolism of purine or synthesis or uric acid and
allantoin. Hyperuricemia (gout). The final breakdown of purines (uric acid, allantoin,
alantoic acid). Catabolism of pyrimidine bases. The final decay of pyrimidines (beta-
alanine, beta-amino isobutyric acid, NH3, CO2).
Biosynthesis of NA. Biosynthesis of purine and pyrimidine nucleotides.
Biosynthesis of polynucleotides of DNA and RNA.
*Ways of synthesis of nucleotides (“saving” way and de novo way). Synthesis of
purine nucleotides, for example, IMP (sequence of reactions). Synthesis of purine
nucleotides (ATP and GTP). Pharmacotherapy: inhibitors of purine synthesis. De Novo
synthesis of pyrimidine. Synthesis of pyrimidine nucleotides (UTP and CTP).
Pharmacotherapy: inhibitors of pyrimidine synthesis. Synthesis of deoxynucletides. De
Novo synthesis of nucleotides. Formation of trinucleotides, polynucleotides of RNA,
DNA. Coding of genetic information. DNA replication (replicating “fork”, stages and
enzymes).
Transcription is the synthesis of RNA (stages: initiation, elongation, termination,
inhibitors of transcription). Reverse transcription. The life cycle of a retrovirus.
Theme of lecture lesson 7. Integration and regulation of metabolism
Metabolism in the organism (common characterstics). Processes of anabolism
and catabolism, and their relationship.
Interconnection of metabolism of carbohydrates, lipids, proteins and nucleic
acids (NA). Interrelation of metabolism of NA and proteins. Interrelation of metabolism
of NA and carbohydrates. Interrelation of metabolism of NA and lipids. Interrelation of
metabolism of proteins and carbohydrates. Interrelation of metabolism of proteins and
lipids. Interrelation of metabolism of carbohydrates and lipids.
*Regulation of metabolic processes (examples).
Thematic Module 3. Metabolism and its reflection in the biochemical parameters
Theme of lecture lesson 1. Reflection of metabolic transformations in
biochemical parameters of blood
Blood biochemistry. Examples of biochemical parameters of animals in normal
and pathological states. pH and buffer systems of blood (for example, different animals).
Chemical and cellular composition of blood. Functions of blood.
*Plasma and serum, their preparation, composition and application.
Theme of lecture lesson 2. Metabolism and its characteristics by biochemical
parametrs of urine
Biochemistry of urine. The production of urine. ‘Thresholds’ and non-
‘Thresholds’ substances of primary urine. Final urine volume (normal, polyuria, oliguria
and anuria.). The chemical composition of urine. The composition of urine in normal
and pathological conditions (pH, cations and anions of urine).
*Examples: indicators of urine in normal and pathological states. Organic
components of normal urine: urea, uric acid, creatinine and creatine, hippuric acid,
indican, amino acids (hyper-amino aciduria) Lactic and pyruvic acid.
The structure of the discipline
Titles of thematic
module and themes
Hours
Full-time Extramural study form
total including total including
L P Labv Ind self L P Labv Ind self
1 2 1 2 1 2 1 2 1 2 1 2 1
Thematic Module 1. Regulatory effects of inorganic and organic substances on the metabolism
Theme 1. Water and
mineral balance and its
effect on the
metabolism
5 2 2 - 1 - - - - - -
Theme 2. Vitamins.
Coenzymes 5 2 2 - 1 - - - - - -
Theme 3. Enzymes and
their kinetic properties 5 2 2 - 1 - - - - - -
Theme 4. Hormones
and mechanisms of
their influence on
metabolic processes
5 2 2 - 1 - - - - - -
Total for the thematic
module 1 20 8 8 - 4 - - - - - -
Thematic Module 2. Dynamic and Functional Biochemistry
Theme 1. Biochemistry
of digestion and
features of digestive
processes in different
organisms
5 2 2 1 - - - - - -
Theme 2. Metabolism
of carbohydrates and its
peculiarities (in
ruminants)
10 4 4 2 - - - - - -
Theme 3. Amphibolic
transformation of
organic substances
(TCAC). Energy of
biochemical processes
5 2 2 1 - - - - - -
Theme 4. Metabolism
of lipids 7 4 2 1 - - - - - -
Theme 5. The
metabolic processes of
proteins and some
amino acids
7 2 4 1 - - - - - -
Theme 6. Catabolism
and anabolism of
nucleotides and nucleic
acids
7 2 4 1 - - - - - -
Theme 7. Integration
and regulation of
metabolism
3 2 - 1 - - - - - -
Total for the thematic
module 2 44 18 18 8 - - - - - -
Thematic Module 3. Metabolism and its reflection in the biochemical parameters
Theme 1. Reflection of
metabolic
transformations in
biochemical parameters
of blood
5 2 2 1 - - - - - -
Theme 2. Metabolism
and its characteristics
by biochemical
parametrs of urine
6 2 2 2 - - - - - -
Total for the thematic
module 3 11 4 4 3 - - - - - -
Course project (work)
__________________
__________________
(if it is in the working
educational plan)
- - - - - - - - - -
Total hours 75 30 30 15 - - - - - -
3. Themes of seminars
There are not planned
# Name of theme Hours
1
2
...
4. Themes of practical classes
There are not planned
# Name of theme Hours
1
2
...
5. Themes of laboratory studies
# Name of theme Hours
1. Regulatory effects of inorganic and organic substances on
the metabolism
Role of mineral substances in the metabolic processes.
Ca quantification by the method of titration. Determination
of concentration of total Calcium in the blood serum by
different methods. Quantification of Fe and Mg in the
tissues. Determination of Phosphorus by the method of
Fiske-Subbarou.
2
2. Biologically active substances, their importance in
metabolism: vitamins
The study of fat-soluble vitamins. Qualitative reactions for
vitamin A: tests with ferric chloride and with sulfuric acid;
for vitamin E: test with nitric acid; for vitamin K.
2
The study of water-soluble vitamins. Qualitative reactions
for vitamins: В1 (thiamine), В2 (riboflavin), В5 (vitamin
РР, nicotinamide), С (ascorbic acid). Quantitative
determination of vitamin C. Quantification of riboflavin
(vitamin B2) in the blood.
3. Enzymes
Effect of temperature and pH on the activity of amylase.
Specificity of enzymes (amylase). Determination of
amylase activity. Effect of activators and inhibitors on
enzyme activity.
Hormones
Effect of hormones on metabolism. Qualitative tests for
hormones, especially tests for adrenaline (sampling with
Iodine and with FeCl3). Effect of adrenaline and insulin on
the level of sugar in the blood. Quantitative determination
of adrenaline and for insulin (tests for estimation of protein
nature of hormone and for presence of S-containing amino
acids). Effect of adrenaline and insulin on sugar level in
the blood.
2
2
4. Thematic Module 1. Regulatory effects of inorganic and
organic substances on the metabolism..
5. Some metabolites of carbohydrates metabolism
Methods of determination of glucose, carbohydrates and
their characterization in the blood. Determination glucose
by enzymatic (e.g. glucosidase) method in the blood.
Quantitative determination of glucose in solution by
Fehling.
Study of properties of polysaccharides (starch, glycogen)
Reaction on the polysaccharides. Observation for colloid
properties of starch. Hydrolytic cleavage of
polysaccharides (starch): e.g. acidic hydrolysis of starch,
hydrolysis of starch by amylase.
Isolation of glycogen by Pfluger method. Hydrolysis of
glycogen. Determination of content of glycogen in the
tissues.
4
6. Biological oxidation of substances and their energetic
exchange
Determination of lactic acid in the blood serum of animals
by colorimetric method and its detection in the muscles,
quantitative determination of ATP in the biological
samples, determination of ATPase activity in the muscle.
Control work: glycolysis, glycogenolysis, fermentation,
pentose phosphate cycle
2
7. Lipids and their metabolites
Study of characteristics of some fats. Detection of fat
(acrolein test) in bio-samples. In biological material,
2
determination of iodine and acid number of fat and other
constants that characterize the quality of fat.
Phospholipids, their characteristics and role in metabolic
processes. Isolation of phospholipids (lecithin) from
biological material and study its physical and chemical
characteristics.
Control work: The Krebs’ Cycle, oxidative
phosphorylation
8. Some amino acids and their metabolism
Isolation of free amino acids from biological fluids and
tissues. Qualitative analysis of amino acids: ‘xanto-
protein’ reaction with aromatic amino acid, tests on
tyrosine, tryptophan, sulfur containing amino acids.
Control work: β-oxidation of Fatty Acids
2
9. Metabolism of proteins
Isolation of proteins from bio-objects: salting proteins,
precipitation of proteins by organic acids and organic
solvents, and their characteristics. Qualitative (biuret
reaction) and quantitative determination of protein by the
method of Lowry.
Control work: transformation of amino acids in the
organism (reactions of trans-amination, deamination,
decarboxylation)
2
2
10. Nitrogen-containing substances and their metabolism
Determination of ammonia in the blood. Determination of
ammonia in the blood by A.I. Silakova’s method.
Determination of uric acid in the blood by colorimetric
method of Myulet-Seifert. Determination concentration of
urea and creatinine content in the biological samples.
Control work: synthesis of urea (ornithine cycle of urea
formation)
2
11. Nucleic acids, their components and metabolites
Isolation of nucleoproteins from the liver of animals or
from other bio-objects and study of their chemical
composition. Isolation of deoxyribonucleoprotein.
Hydrolysis of nucleoprotein. Detection of DNA in
deoxyribonucleoprotein.
Nucleic acids, their components and metabolites
Nucleic acids, their isolation from hydrolysates of liver
tissue and/or yeast. The biuret reaction on the presence of
peptide bonds in nucleoproteins. The test on the purine
bases derived from hydrolysis of nucleoproteins in the
presence of acid. Qualitative determination of the
carbohydrate component in the hydrolyzate nucleoprotein:
Trommer's test, Fehling, Tollens (on pentoses). Qualitative
reaction on the presence of phosphoric acid in hydrolyzate
2
of nucleoproteins.
Control work: Synthesis of Uric Acid
12. Thematic Module 2. Dynamic and Functional
Biochemistry
13. Metabolism and its reflection in biochemical parameters
Blood. Some biochemical parameters.
Isolation of blood serum and plasma. Determination of
Heme in Hemoglobine of blood by reaction with benziine
and guaiacol. Quantative determination of Hemoglobine in
the blood.
Biochemical parameters of urine
Determination of color, transparency, odor, specific
gravity, pH, acidity and alkalinity of the urine.
Quantitative determination of the acidity of urine.
Qualitative reaction for creatinine. Determination of
inorganic components of normal urine (chlorides, sulfates,
phosphates). Determination of pathological components of
urine with pathologies (test on protein, sugar, pigments,
acetone bodies)
2
14. Biochemical parameters of milk
Isolation serum of the milk. Sedimentation and isolation of
casein. Determination of acidity of milk. Qualitative
analysis of milk components (test on casein, determination
of albumins and globulin, determination of lactose,
determination of Calcium, chlorides, phosphates, sulfates.
Determination oxido-reductase activity in the milk.
2
15. Thematic Module 3. Metabolism and its reflection in
biochemical parameters
Total hours 30
6. Test question, the tests sets to determine the level assimilation of knowledge by
students.
1. Formation of ethanol amine (in the activated form)
2. Build right chain of reactions of the urea cycle from citrulline
3. Build right chain of reactions of the urea cycle from urea
4. Build right chain of reactions of the urea cycle from arginine
5. Build right chain of reactions of the urea cycle from ornithine
6. What class of vitamins do the substances belong to?
7. How does somatotropin influence gluconeogenesis in the liver?
8. Functional biochemistry does study...
9. Glycerol oxidation: glycerol phosphokinase reaction (it’s necessary to choose substrates
and products).
10. What peculiarities of baby-digestions (it’s about enzymes in the different compartments of
digestion-tract?
11 It’s necessary to write names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented
by one reaction here).
12 Under transamination of pyruvate, it is formed such important substrate of
gluconeogenesis as ...
13 Distraction of phospholipids: it’s necessary to give characteristic of reaction that
catalyze by phospholipase D (substrates, products).
14 How it could be lowered the glucose level in the dog’s blood (under conditions of
diabetus mellitus)?
15 Lactic acid fermentation: under fermentation by Bact. lactis, lactic acid is formed from
glucose: C6H12O6 -> 2 CH3-CHOH-COOH;
16. ... is compartment of such enzymes as carboanhydrase, uricase, urease, aldolase, and
phosphatase.
17. What enzyme does digestion of proteins?
18. Glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis:
19. (NAD-dependent) isocitric acid reaction of TCAC:
20. Enzymes can be consisted of what class of organic substances? Enzymes can be
consisted o f . . .
21. What function do biological membranes in animal organism?
22. ‘Philohinon’ and ‘pharnohinon’ are natural forms of vitamin ...
23. What is modification of the ‘key-lock’model which is characterized enzymatic action?
24. What enzymes do hydrolysis of the nucleic acids component of nucleoproteins?
25. Who was the first scientist that showed importance of vitamins?
26. Role of water-soluble vitamins, especially vitamin P:
27. What reaction is catalyzed by hydrolases?
28. What enzymes do ‘digestion’ of lipids?
29. What coenzyme takes part in the reaction of formylation and formation of methyl-
groups?
30. What element takes part in the process of oxidative phosphorylation?
31. It’s necessary to choose a name of biological active substance which is catalyzed by
chemical processes in the organism
32. It’s necessary to choose substrates and products of the carbamoyl phosphate synthase
reaction of the urea cycle (substrates, products)
33. What is the second irreversible reaction of glycolysis (according to the name of
enzyme)?
34. Formation of choline (in the activated form):
35. Build right chain of reactions of the TCAC starting from a-ketoglutarate:
36. Build right chain of reactions of the TCAC starting from succinate
37. Build right chain of reactions of the TCAC starting from succinyl-CoA
38. Build right chain of reactions of the TCAC starting from fumarate
39. Build right chain of reactions of the TCAC starting from malate
40. Build right chain of reactions of the TCAC starting from oxaloacetate
41. Build right chain of reactions of the TCAC starting from citrate
42. Build right chain of reactions of the TCAC starting from isocitrate
43. All pointed out carboxylic acids belong to …
44. Cortisol (which is belonged to glucocorticoids) ... gluconeogenesis.
45. Static biochemistry does study...
46. What peculiarities of digestions in ‘mature’ animals (it’s about enzymes in the different
compartments of digestion-tract)?
47. It is necessary to choose names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented by
one reaction here; substrates, products, enzyme, coenzyme).
48. Synthesis of TAG. It’s necessary to choose right reaction of glycerol-3-phosphate
formation by glycerol phosphokinase (substrate, products).
49. Catabolism of the sterol esters by enzymes (It’s necessary to choose typical reaction with
the pointed out substrates, products and enzyme).
50. Substrate phosphorylation in the TCAC is carried at step of transformation o f . . .
51. Alcoholic fermentation and its brief characteristics.
52. Role of Sodium in the animal life:
53. Glycolysis. It’s necessary to choose names of substrates and products of the reaction
catalyzed by ‘phosphoglycerate kinase’
54. The reaction of the TCAC is catalyzed by multi-enzyme complex of α-ketoglutarate
dehydrogenase (substrates and products):
55. Biological role of vitamins.
56. Biological role of fat-soluble vitamins.
57. Biological role of water-soluble vitamins.
58. Biological role of vitamin A.
59. Biological role of vitamin E.
60. Biological role of vitamin K.
61. Biological role of vitamin D.
62. Biological role of vitamin Bl.
63. Biological role of vitamin B12.
64. Biological role of vitamin B5.
65. Biological role of vitamin C.
66. Formation of histamine is ...
67. What enzymes do digestions of polysaccharides?
2
68. What microelement is in a structure of hemoglobin, or myoglobin, or cytochromes?
69. Role of water-soluble vitamins, especially C.
70. How does enzyme work concerning the energy reaction activation (Ea)?
71. What enzymes do digestion of lipids?
72. Role of Nitrogen in the animal life:
73. The substances as ... belong to vitamin F.
74. What reaction does catalyze by lyase?
75. What enzymes do digestion of carbohydrates?
76. Who showed the enzyme activity dependence of pH of medium?
77. Enzymes of protein synthesis are localized mostly in ...
78. Zinc is belonged to ...
79. Biosynthesis of urea is in the...
80. What is the third irreversible reaction of glycolysis (according to the name of enzyme)?
81 Phosphoglycerate mutase reaction of glycolysis (at the end of the tests)
82 Build a chain of chemical transformations in the glycolysis starting from hexose
83 In the table, enzymes take part in the processes of...
84. The ... biochemistry does study the transformation of substances up to the end-
products of metabolism
85. β-oxidation of fatty acids: what is going on in reaction catalized by carnithine
acyltransferase I?
86. In the humane organism, it’s founded Cu-deficit that causes lowering enzyme activity
of . . .
87. Role of choleic acid in digestion of lipids:
88. Role of fat-soluble vitamins, especially vitamin F.
89. Localisation of processes of β-oxidation (activation of FA and actually their β-oxidation):
90. Alcali reserve of blood mainly is ...
91. Glycerol oxidation: glycerolphosphokinase reaction (it’s necessary to choose substrates
and products).
92. What peculiarities of baby-digestions do you know (it’s about enzymes in the different
compartments of digestion-tract)?
3
93. It’s necessary to write names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented by
one reaction here).
94. Under transamination of pyruvate, it is formed such important substrate of
gluconeogenesis as ...
95. Distraction of phospholipids: it’s necessary to give characteristic of reaction that
catalize by phospholipase D (substrates, products).
96. How it could be lowered the glucose level in the dog’s blood (under conditions of
diabetus melitus)?
97. Lactic acid fermentation: under fermentation by Bact. lactis, lactic acid is formed from
glucose: C6H,206 2 CH3-CHOH-COOH;
98 … is compartment of such enzymes as carboanhydrase, uricase, urease, aldolase, and
phosphatase.
99. What enzyme does digestion of proteins?
100. Glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis:
101. (NAD-dependent) isocitric acid reaction of TCAC:
102. Enzymes can be consisted of what class of organic substances? Enzymes can be
consisted of...
103. Role of Selenium in the animal life:
104. What is biological importance of glucose-lactate cycle?
105. What is biological importance of the pentose phosphate pathway fuctioning in the
erythrocytes?
106. Role of Ferum in the animal life:
107. The reaction of the TCAC is catalized by succinyl thiokinase (substrates and
products):
108. Carotenoids are precursors of ... vitamin
109. What is remarkable characteristic of urease?
110. What enzymes do digestion of oligosaccharides?
111. What disease progresses under conditions of Iodine deficit in diet?
112. What class of enzyme does El belong to (according Enzyme Classification)?
4
113. What name of substances are under “3” in the scheme of synthesis of uric acid?
114. What enzymes do digestion of phospholipids?
115. What is “a main purpose” of ornithine cycle?
116. Under transamination of oxaloacetate, it is formed such important substrate of
gluconeogenesis as ...
117. What reaction is catalyzed by isomerase?
118. What enzymes do digestion of proteins?
119. Enzymes of cellular respiration are mainly localized in ...
120. Butyric acid fermentation:
121. Sodium exchange is regulated by ...
122. Ornithine transcarbomoyl transferase reaction of the urea cycle (substrate and
products)
123. Increase secretion of adrenaline leads to ... glucose level in the blood
5
National University of Life and Environmental Sciences of Ukraine
EQL Bachelor
Direction of training
110101
Specialty _________
Veterinary Medicine
Department of
Biochemistry of Animals,
Quality and Safety of
Agricultural Products
20__-20__ educational.
year
EXAM TEST № _1_
of discipline
Biochemistry of Animals
with the Fundamentals of
Fhysical and Colloid
Chemistry
Confirm Acting as Heads
________________
(signature)
Tomchuk V.А._(Fn,Init)
____________20___
Examination questions
(The maximum score is 10 points for every question)
1. What participants of TCAC reaction precede the formation of malate?
2. Create a series of changes to the ribosome during protein biosynthesis, where the last step was the formation
of peptide bond
Tests of various types
(The maximum score is 10 points for answers to tests)
1 Below pointed compounds can be called ..
…
AMP ADP ATP CMP GMP GDP
UDP UMP UTP CDP CTP GGP
(in the form of answers write in short)
2. Synthesis of TAG: Describe diacylgycerol-acyltransferase reaction (substrates, products). A) phosphatidic acid → 1,2-diacyl glycerol + Pi
B) dyoxyacetonphosphate + NADH + + H
+ → glycerol-3-phosphate + NAD
+
C) phosphatidic acid + acyl-CoA → 1,2-diaсyl glycerol + CoASH
D) glycerol-2-phosphate → glycerol-3-phosphate
E) 1,2 diacylglycerol + acyl-CoA → triacyl glycerol + CoASH
3. . The first stage of pentose phosphate pathway is called ...
4. How are monoacyl glycerols absorbed? A) monoacyl glycerols are absorbed by simple diffusion;
B) monoacyl glycerols are absorbed by pinocytosis;
C) monoacyl glycerols are absorbed by simple diffusion or pinocytosis;
D) monoacyl glycerols are absorbed in combination with bile acids;
E) monoacyl glycerols are absorbed by phagocytosis;
5. What are 3 reactions in glycolysis irreversible? A) mutase, phosphofructokinase, pyruvate kinase reactions
B) hexokinase, phosphofructokinase, pyruvate kinase reactions
C) hexokinase, phosphofructokinase, lactate dehydrogenase reactions
D) hexokinase, aldolase, pyruvate kinase reactions
E) triosophosphate isomerase, aldolase, enolase reactions
6. What level of the Pentose Phosphate Pathway function effectiveness is in the tissues with a predominance of
oxidative metabolism (for example, sceleton muscles)?
A) high level;
B) low level;
C) stable low level; D) the depressed level;
E) no changes
7. Glucokinase reaction of glycolysis.
A) substrate: phosphoenol pyruvate, ADP, H2O; product - pyruvate, ATP
B) substrates: glyceraldehyde-3-phosphate, Pi, NAD +; products - 1.3 diphosphoglycerate, NADH (H
+);
C) substrates: 1.3 diphosphoglycerate, ADP, NAD+; products - 3-phosphoglycerate, ATP;
D) substrate: glucose, ATP; product - glucose-6-phosphate, ADP;
E) substrate: 2-phosphoglycerate, H2O; product - phosphoenol pyruvate
8. Fumarate hydratase (fumarase) of TCAC reaction has …
A) substrates: isocitrate, NAD+; products: α-ketoglutarate, NADH (H
+), CO2;
B) substrates: succinate, FAD; products - fumarate (trans-compound) FADH2;
C) substrates: acetyl-CoA, oxaloacetate, H2O; products - citrate, CoA-SH;
D) substrates: isocitrate, NAD+; Products: alpha-ketoglutarate, NADH (H
+);
E) substrates: fumarate, H2O; Product: Malate;
9. What enzymes do digestion of carbohydrates?
A) protease, trypsin, pepsin, transferase;
B) phosphodiesterase, nukleozidase, ligase
C) lipase, phospholipase, holesterol esterase
D) amylase, succrase, maltase, celobiase
E) nuclease, lipase, amylase
10. Microelement (that has antioxidant properties) is involved in oxidative phosphorylation, along with vitamins
E and produces radioprotective effect, and there is:
A) Zn B) Co C) Mo D) Mn E) Se
6
Methods of teaching
Methods of teaching (methods (greek) - ‘a way of knowing the way of finding
the truth’) - the streamlined ways of the interrelated, purposeful activity of the teacher
and students for the effective resolution of problems of study discipline "Biochemistry
of Animals with Fundamentals of Physical and Colloidal Chemistry". Methods of
teaching are implemented via the system of instruction (actions of teacher and students,
implemented the requirements of various methods) and of training activities (various
training equipment used in the system of cognitive activity: books, laboratory
equipment, facilities).
Below are teaching methods used on core classroom training sessions of
discipline "Biochemistry of Animals with Fundamentals of Physical and Colloidal
Chemistry" and during independent work of students.
By source and nature of the transmission of information perception, generally,
there are three groups of teaching methods:
verbal (narrative, explanation): the story is a method of study involving
narrative, a descriptive form of disclosing educational material (involving
imagination of student); explanation is the verbal learning method (whereby the
teacher reveals the essence of a phenomenon, the law of the process), based on
logical thinking with prior experience of students;
visual (demonstration, illustration): demonstration is a method of teaching
which involves showing objects and processes actually in dynamics; illustration
is a method of teaching in which objects and processes are revealed through their
symbolic images (photographs, drawings, charts, graphs etc.)
practical (laboratory method, practical work, exercise, observation): laboratory
method involves the organization of training activities through the use of special
equipment and specific technologies for acquiring new knowledge or test
scientific hypotheses at the level of research; practical work aims to use the
knowledge gained in the resolution of practical tasks (for example, performing
some kind of experiment or its fragment in biochemical research of scientists);
exercise is a method of teaching, the essence of which is to deliberate, repetition
by students some actions or operations to the formation of skills (for example,
ability to use machinery and equipment of biochemical laboratory); observation
as a method of training involves perception of certain objects, phenomena and
processes in natural and laboratory environment without interfering with these
phenomena and processes.
Studying the structure, physico-chemical and biological properties of natural
compounds, their metabolism, regulation and correction of metabolic processes by
exogenous and endogenous factors used the teaching methods that are different in
character logic of knowledge, namely:
7
- analytical method that involves thinking or practice schedules whole into parts in
order to study their essential features;
- inductive method, which is the way of examining objects, events from the unit to
the total;
- deductive method, based on a study of educational material from general to
specific, single;
- ‘traduktyvnyy’ method that provides findings from individual to individual, and
the particular to the particular, from the general to the general.
The above methods are used on core classroom training sessions of (see below)
subject "Biochemistry of Animals with Fundamentals of Physical and Colloidal
Chemistry".
The main types of lessons of discipline "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" are the classes: auditorium classes
(lecture, laboratory sessions, and consultations) and independent study of students.
Educational Lecture of discipline "Biochemistry of Animals with Fundamentals
of Physical and Colloidal Chemistry" is logically verified, scientifically sound and
systematic exposition of scientific questions that cover the structure, physico-chemical
and biological properties of natural compounds, their metabolism, regulation and
correction of metabolic processes using a fodder and medicines to strengthen health and
improve animal productivity. Lecture course "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" is illustrated and presented in a
presentation (PDF-files are provided to students) to better absorption of the material.
As the lecture is one of the main types of classes and simultaneously teaching
methods in higher education, it is intended to form a basis of knowledge of students in
biochemistry of animals and fundamentals of physical and colloid chemistry, as well as
determine the direction, the main content and nature of laboratory work and
independent students' work on the subject "Biochemistry of Animals with Fundamentals
of Physical and Colloidal Chemistry".
Laboratory lesson is a type of instruction where under the guidance of the
teacher, students conduct real or model experiments or experiments in specially
equipped training labs using equipment suited for the educational process. Herefrom,
didactic purpose of laboratory studies is the practical proof of certain theoretical
positions subject "Biochemistry of Animals with Fundamentals of Physical and
Colloidal Chemistry", the acquisition of practical skills and experience working with
complex equipment, equipment, computers, instrumentation, experimental methods of
biochemical research.
Stages of preparation and conduct laboratory class are: pre-control training of
students in a particular laboratory work; specific tasks in accordance with the proposed
theme, design custom reports, assessment results of student by teacher.
It must be noted that in the case of laboratory work relating to the possible danger
8
to the health and lives of students, a mandatory step in its preparation and conduct are
instructed on safety rules and monitoring their compliance, conducted as the first lesson
(general instruction work in biochemical laboratories), and these (training on individual
possibly dangerous conditions of the experiments).
Consultation is one of the types of classes that is conducted to obtain student
responses to some theoretical or practical aspects of biochemistry animals and to clarify
certain aspects of the theoretical principles or their application in veterinary medicine.
Consultations during the semester (current consultations semester) and before control
measures (exam) held on schedule of Dean's office.
Independent work or self-work is the primary means of learning student
educational material on the biochemistry of animals at the time free from mandatory
training sessions. In this course, an independent work or a self-work is performed as a study of the
use of methods, methodological approaches and techniques based on published research
materials in the form of books, manuals, guidelines, patents, etc. (*it’s pointed themes
of self-work in the thematic material of lectures).
Methods of teaching in terms of independent mental activities:
- the problem statement, which provides for the creation by a teacher the
problematic situation, help students in the selection and "acceptance" problem task;
- partial search method that involves students in finding ways, methods and means
of resolution of cognitive tasks;
- research method that aims to include students in independent resolution of
cognitive tasks with the necessary equipment.
Forms of control
For application and by nature, control is divided into the previous, current,
periodic, final, mutual control, self-control. Previous monitoring conducted to determine the level of preparedness of
students for the new school year or semester. The results of this control significantly
affect the initial clarification of the situation to further the educational process in higher
education, detalisation, optimization and more focused definition of its semantic
component, substantiation of sequence processing sections and parts of the course
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry",
determination of basic techniques, forms and means of its implementation, etc.
Current control is used for testing as individual students, as academic groups,
usually in their daily learning activities, primarily for scheduled classes. The teacher
systematically observes students' academic work, checks the level of mastery of the
program material, the formation of practical skills and abilities, experience skills, but
also presents the corresponding estimates for oral answers, tests, practical laboratory
experiments (protocol implementation which are presented in a workbook on the subject
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry",
Part 1 and Part 2), provided by the discipline.
9
Current control is educational in nature, as is aimed at stimulating students' desire
to systematically work independently of educational material, to raise their level of
knowledge and to improve the teaching skills of teachers.
Periodic monitoring (ranking with thematic modules) is a systematic, planned
and focused. It consists in determining the level and extent of mastery of knowledge,
skills and abilities late as thematic modules, and a time interval: week, month, quarter,
etc. This control is carried out in the course of routine activities (exercises), and
designated backup time.
Summative assessment (test, exam) aims to determine the level of fulfillment of
the tasks set out in the curriculum, training plan and other documents that govern the
educational process. It covers both theoretical and practical training for students, spend
it, usually at the end of the second semester (test) and third (test) as well as during
special events check.
In the educational process of the study subject "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" works in the form of mutual advice,
consultations, exchange of experience, best students help those who lag behind in
education.
Important means of control is self-control which implements the practice of the
principles of activity and consciousness, strength of knowledge, skills and abilities of
students.
There are two forms of self-control: individual and group. In case of individual
forms of control, student determines the degree of mastery of professional knowledge;
skills and abilities (most offer student objectively assesses their response). Group
provides self-assessment of their learning activities and progress achieved, as well as
the identification of weaknesses, study ways to overcome them (widely practiced in the
performance of laboratory work, exploratory theoretical work that allows students to
deepen their knowledge on a particular topic).
The main forms of test knowledge and skills, in addition to self-control, are
individual, frontal and group check.
The purpose of individual test is to determine at what level each student mastered
a complex of knowledge and skills, the development of professional skills, and to
identify major shortcomings and ways to address them.
Frontal test applied to a relatively short period of time to find out the level of
mastery of the program material. Teacher prepares particular topic short questions for
students to demand short answers to them from the place. For example, the front
paperwork.
Group test aims to determine the level of collective action, coherence and
cohesion during the tasks.
Sometimes it pays off combined test - a combination of the above forms.
According to the control objectives that define teachers to implement these types
of checks, there are used certain methods.
Methods of test are set of techniques and methods of pedagogical diagnostic
efficiency of teaching and learning of students to ensure full and meaningful
10
information about the didactic process in universities and on their effectiveness and
efficiency.
Basic methods of checking students' progress in the didactic process and
determine the effectiveness of this process:
- comprehensive monitoring,
- written works,
- oral interviews,
- practice,
- didactic tests,
- programmable control, etc.
Using the method of observation of teaching and learning activities of students
during the study subject "Biochemistry of Animals with Fundamentals of Physical and
Colloidal Chemistry", teacher knows the details of their activities (both in class and
outside of classroom time - when performing tasks of independent work attitude, will
and desire to study biochemistry, fundamentals of physical and colloidal chemistry),
finds inclinations and abilities, success, behavior, capabilities and ways of acting in
certain situations (such as when performing laboratory experiments), defines the scope
and depth of mastery of professional knowledge, the level of mastery relevant skills and
abilities, degree of formation of merit, determines shortcomings and ways to address
them more. Monitoring survey can be done at any time and for any classes.
Written control provides deep and comprehensive mastery test of program
material. With written work, there is simultaneously control of a large number of
students. This method is fairly objective, because it gives the opportunity to compare
different knowledge students using standard questions, identify theoretical knowledge,
practical skills and adequate applications for solving specific professional tasks (such as
the use of biochemistry in the practice of veterinary physician). In this analysis, the
teacher formed of each student about his strengths and weaknesses.
Objective and comprehensive analysis has a very strong educational and didactic
effect as on scientific and educational worker as on other students.
One of the testing methods is an oral survey carried out by means of interviews,
stories of student, interpretation of certain theories, ideas, opinions of professional
events and more. The biggest methodological value of oral questioning is to provide
direct live contact with the teacher learners. The basis of oral questioning is
monological answer of student or conversation. This method, due to its specificity and
the nature of the application, is used as a daily classroom routine, and the various
checks.
During the survey, special attention should be paid to the formation of benevolent
moral and psychological atmosphere in the group that interview. Initially, the teacher
clearly articulates the question, and only after a pause (15 - 20 seconds) determines the
student who has to answer. There is also practiced student to ask questions correctly,
including oral responses of other students or performances. Ability to set clear student
11
questions also indicates good possession educational material, in this case points to
deeper knowledge on relevant topics of biochemistry.
Usually, there is a higher grade deserving by students who actively offer
innovative solutions to this or that problem when studying the biochemistry of animals.
In case of failure of the student immediately give the correct answer, his thinking should
be directed in the right direction, prompting skill required direction finding correct
answers.
Very effective method of verifying the students is a method of practicing, for
example, at laboratory studies: the practice of working with instruments and devices of
biochemical laboratory, practice of proper use of laboratory equipment, etc.
In didactic practice, there is increasingly using didactic tests those are
standardized set of tasks to specific educational material through which define the level
of mastery. Tests allow you to objectively assess the level of mastery of theoretical
knowledge, practical skills and abilities.
For training purposes, tests are divided into four types:
verification of knowledge (facts, concepts, laws, theories), ie knowledge of
information that was necessary to continue to remember and now reproduce. The
main thing here is the reproduction of knowledge;
identify skills to perform certain mental actions based on acquired knowledge.
Requires ability to solve common tasks;
identify their own skills to make a critical analysis of the material studied;
identifying the skills students creatively use the knowledge in solving non-routine
tasks.
In higher education institutions, there are also beginning to be used for
monitoring and assessing students programmable control. This broad possibility give
computers that provide immediate feedback between the response of the trained and
programmed learning material, allow immediately get information about the level of
response.
Method of machine (programmable) control is carried out by means of electronic
computers and control programs. The computer is the most objective controller in the
study all subjects. Software controls are made up according to the method of control of
programmed exercises; answers are typed as numbers or formulas. However, the
machine can not take into account the psychological characteristics of the student; can
not completely replace the teacher, especially in a timely manner to assist him in case of
difficulties with choosing the correct answer.
Method of test control can be out of engine (under condions of not using
computer) and engine (under condions of using computer). The basis of such control are
12
tests - special tasks performance (or failure) of which indicates the presence (or
absence) in the students certain knowledge, skills.
To control the quality of the knowledge and skills students study subject
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry"
traditionally used: individual interviews, tests, modular work, colloquia, tests, exams
etc.
10. Distribution of points that get students. Evaluation of the student is in
accordance with the provisions of "On the examinations and tests NUBiP in
Ukraine" dated 02/20/2015. The protocol number 6 from the table. 1.
National
estimation ECTS
Evaluation ECTS Definition of evaluation
Rating student,
points
“Excellent” А Excellent - excellent performance with few
errors 90 100
“Good”
В VERY GOOD - above average with some
mistakes 82 89
С GOOD - generally correct work with a
number of gross mistakes 74 – 81
“Satisfactory
”
D Satisfactory - not bad but many drawbacks 64 73
Е ENOUGH - performance meets the
minimum criteria 60 – 63
“Unsatisfacto
ry”
FX Unsatisfactory - must work before get
credit (positive evaluation) 35 59
F Poor - thorough and elaborate 01 34
Rating from attestation is determined on a 100 ball scale and includes rating from a
test, that calculation Rtest. = 30.0 points, which settles accounts after a formula:
Rat.= 0.3 ∙ Rtest.
For determination of the real rating from discipline it is necessary to make the
marks collected during an educational semester:
R = 70 + 30 = 100 points.
13
11. Methodical maintenance
1. Methodical recommendations to laboratory classes on «Biochemistry of animals
with fundamentals of physical and colloidal chemistry» for students of Faculty of
Veterinary Medicine; Part I; Physico-chemical methods in biochemical
investigation / С.Д. Мельничук, Л.Г. Калачнюк // Методичні рекомендації. К:
Видавничий центр НУБіП України, 2013. – 149 с.
2. Методичні рекомендації до виконання лабораторних робіт з дисципліни:
«Біохімія тварин з основами фізичної і колоїдної хімії» для студентів
факультету ветеринарної медицини. Методичні рекомендації / С.Д.
Мельничук, Л.Г. Калачнюк, Г.І. Калачнюк, Л.В. Кліх. К: Видавничий центр
НУБіП України, 2013. – 148 с.
3. Закон України "Про вищу освіту" // Держава і право. – 2002. – № 43.
4. Національна доктрина розвитку освіти // Освіта України– 2002. – 23 квітня.
5. Алексюк А. М. Педагогіка вищої школи. Історія. Теорія. Курс лекцій:
модульне навчання. – К., 1993.
6. Васянович Г.П. Педагогіка вищої школи Навч.‐ метд. посібн. – Львів, 2000.
7. Кузьмінський А.І. Підагогіка вищої школи.: Навч. посіб. – К., 2005.
8. Педагогіка вищої школи. Навчальний посібник. – Одеса: ПДПУ імені К.Д.
Ушинського, 2002.
9. Фіцула М.М. Педагогіка вищої школи: Навч. посіб. – К., 2006.
10. Шейко В.М., Кушнаренко Н.М. Організація та методика
науково‐дослідницької діяльності: Підручник. – К., 2006.
11. П’ятакова Г.П. Технологія інтерактивного навчання у вищій школі.
Навчально ‐ метод. посібник. – Львів, 2008
12. Дичківська І.М. Основи педагогічної інноватики навчальний посібник. –
Рівне: РДПУ. 2001. – 233 с.
13. Дичківська І.М. Інноваційні педагогічні технології. Навч. посібник. – К.:
Академ.видав., 2004. – 352 с.
14. Андрущенко В. Високі педагогічні технології / В. Андрущенко, В. Олексенко
// Вища освіта України. - 2007. - № 2. - С. 70 -76.
15. Пінчук О. Проблема визначення мультимедіа в освіті: технологічний аспект //
Нові технології навчання. - К., 2007. - Вип. 46. - С. 55 - 58.
16. Гончаров С.М. Інтерактивні технології навчання в кредитно-модульній
системі організації навчального процесу: Навчально-методичний посібник. -
Рівне: НУВГП, 2006. - 172 с.
17. Бабанский Ю.К., Поташник М.М. Оптимизация педагогического процесса: В
вопросах и ответах. - 2-е узд., переработанное и доп. - К., 1984.
18. Вища освіта України і Болонський процес: Навчальний посібник / За
редакцією В.Г. Кременя, Авторський колектив: М.Ф. Степко, Я.Я. Болюбаш,
В.Д. Шинкарук, В.В. Грубінко, І.І. Бабин. - Тернопіль: Навчальна книга -
Богдан, 2004. - 384 с.
19. Болюбаш Я.Я. Організація навчального процесу у вищих закладах освіти:
Навч. посібник для слухачів закладів підвищення кваліфікації системи вищої
освіти.— К.: ВВП «КОМПАС», 1997.— 64с.
14
12. Recommended Literature
- Basic;
1. Біохімія: практикум / Д.О. Мельничук, С.Д. Мельничук, Л.Г. Калачнюк, Г.І.
Калачнюк. За загальною редакцією академіка НАН України і НААН Д.О.
Мельничука (рекомендовано Міністерством освіти і науки, молоді та спорту
України, лист № 1/11-16887 від 30.10.2012) - К: ВЦ НУБіП України, 2012, 528 с.
2. Маршалл В.Дж., Бангерт С.К. Клиническая химия. 6-е изд.: Пер. с англ. М:
Бином, 2011. – 408 с.
3. Фаллер Дж.М., Шилдс Д. Молекулярная биология клетки. Руководство для
врачей. Пер. с англ. М: Бином-Пресс, 2011. – 256 с.
4. Кольман Я., Рем К.-Г. Наглядная биохимия. 3-е изд.: Пер. с нем. М.: Мир, 2009.
469 с.
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