- •Биологическая химия
- •060101 – Лечебное дело
- •Часть II
- •Contents
- •Cholesterol
- •I. Theoretical part
- •1. Lipids metabolism
- •1.1. Classification of lipids
- •2. Glycolipids (basically glycosphingolipids).
- •Galactosyl ceramide
- •1.2. Digestion and absorption of fats
- •Lipolysis of triglycerides in adipose tissue
- •1.3. Fatty acids oxidation
- •2. Transport of fa inside mitochondrion.
- •3 Ketocyl CoA tyolase Palmitic acid preformed rest Palmityl-CoA Acetyl-CoA
- •Oxidation of unsaturated fatty acids
- •Violations of fatty acids oxidation
- •Acetyl-CoA metabolism
- •1.4. Lipogenesis
- •Regulation of fatty acids synthesis and break down
- •1.5. Metabolism of phospholipids
- •1.6. Essencial fatty acids. Eicosanoids
- •1.7. Cholesterol metabolism
- •Distribution and functions of cholesterol
- •Cholesterol biosynthesis
- •1. Conversion of active acetate into mevalonic acid.
- •2. Squalene formation from mevalonic acid.
- •Regulation of cholesterol synthesis
- •Cholesterol esters metabolism
- •Synthesis of bile acids
- •1.8. Regulation of lipid metabolism
- •1.9. Violations of lipid metabolism
- •Violation of fats adsorption processes:
- •Test questions
- •2. Proteins metabolism
- •2.1. Pathways of proteins degradation
- •2. Digestion of proteins.
- •The selectivity of peptidases
- •2.2. Amino acids metabolism
- •The reactions of amino groups
- •Intramolecular deamination.
- •Reactions of the carboxyl group
- •2. Aminoacyladenylate formation.
- •2.3. Ammonia neutralization in the body
- •Storage and transport of ammonia
- •Fumarate pyruvate aspartate
- •2.4. Violations of nitrogen metabolism
- •2.5. Metabolism of individual amino acids
- •2. Metabolism of sulfur amino acids.
- •3. Metabolism of branched chain amino acids.
- •Leu, Ile, Val α-keto acids acyl-CoA derivatives
- •4. Metabolism of dicarboxylic amino acids
- •5. Metabolism of diaminomonocarboxylic acids.
- •6. Metabolism of phenylalanine and tyrosine.
- •7. Metabolism of tryptophan.
- •2.6. Metabolism of conjugated proteins. Chromoproteins metabolism
- •The degradation of hemoglobin in the tissues (the formation of bile pigments)
- •The hemoglobin biosynthesis
- •2.7. Nucleoproteins metabolism
- •Adenine hypoxanthine; guanine xanthine
- •The synthesis of pyrimidine nucleotides u, c, t
- •I nosine-5'-phosphate Xantosine-5'-phosphate
- •The synthesis of deoxyribonucleotides
- •Test questions
- •3. Template biosynthesis
- •3.1. Biosynthesis of nucleic acids
- •3.1.1. Dna biosynthesis (replication)
- •Synthesis of dna in the rna template
- •3.1.2. Rna biosynthesis
- •Rna synthesis in rna template
- •3.2. Protein biosynthesis
- •The properties of the genetic code
- •Preparatory stage of protein synthesis
- •3.2.1. Translation
- •1. Initiation.
- •2. Elongation.
- •3.2.2. Post-translational modification of proteins
- •Transport of synthesized proteins through membranes
- •3.2.3. Regulation of protein biosynthesis
- •3.3. Genetic engineering
- •Test questions
- •4. Hormones, nomenclature, classification
- •Test questions
- •5. Metabolic processes interaction
- •In the organism
- •Protein and carbohydrate metabolisms interconnection
- •Protein and lipid metabolisms interconnection
- •Carbohydrate and lipid metabolisms interconnection
- •Levels of homeostasis regulation
- •Changes in metabolism during starvation
- •Test questions
- •6. Mineral and water and salt metabolism
- •6.1. Water in the human body
- •6.2. Salt metabolism
- •7. Renal biochemistry. The role of the kidneys in the regulation of water and salt metabolism
- •7.1. Excretory function of the kidneys
- •7.2. Homeostatic function of the kidneys
- •7.3. Metabolic functions of the kidneys
- •7.4. Regulation of water and salt metabolism and uropoiesis
- •Test Questions
- •8. Biochemistry of nervous tissue
- •8.1. Features of metabolism of nervous tissue
- •8.2. Mechanism of nerve impulses conduction
- •Cholinergic synapses
- •Test Questions
- •9. Biochemistry of muscle tissue
- •9.1. Chemical composition of muscle tissue
- •Sources of energy for muscle work
- •9.2. Mechanism of muscle contraction and its regulation
- •9.3. Biochemical changes in muscles within pathology
- •Test Questions
- •10. Biochemistry of extracellular matrix
- •10.1. Structure of extracellular matrix
- •Collagens.
- •Fibril-forming collagens
- •Collagen, forming a tela
- •10.2. Features of metabolism of extracellular matrix Catabolism of extracellular matrix proteins
- •Reparation of damage of the extracellular matrix in norm
- •Biochemical changes of connective tissue with aging
- •The lesions of connective tissue
- •11. Blood biochemistry
- •11.1. Respiratory function of blood. Buffer systems of blood
- •11.2. Blood coagulation system. Changes in pathology
- •Extrinsic and intrinsic pathways of blood clotting
- •Test Questions
- •12. Liver biochemistry
- •12.1. Main functions of the liver
- •The role of the liver in the metabolism of carbohydrates
- •The role of liver in lipid metabolism
- •The role of the liver in the metabolism of proteins and amino acids
- •12.2. Choleresis. Pigment metabolism. Types of jaundice
- •The cleavage of hemoglobin: hemoglobinverdoglobinbiliverdinbilirubin.
- •12.3. Detoxifying liver function
- •Test Questions
- •13. Regulation of calcium and phosphorus metabolism
- •14. Bone biochemistry
- •Test Questions
- •II. Laboratory workshop Laboratory work 1. Lipid metabolism
- •Hydrolysis of milk fat by lipase
- •Test Questions
- •Laboratory work 2. Phospholipids. Cholesterol
- •4.1. Schiff reaction.
- •4.2. Salkowski reaction.
- •4.3. Lieberman-Burchard reaction.
- •Preparation of solutions of cholesterol for the calibration curve
- •Test Questions
- •Laboratory work 3. Digestion of proteins. Determination of acids of gastric contents
- •Experiment 2. Qualitative determination of free hydrochloric acid in gastric juice using indicator congo red.
- •Results of the determination of gastric acidity
- •Test Questions
- •Laboratory work 4. The end products of nitrogen metabolism
- •Test Questions
- •Laboratory work 5. Hormones
- •2.1. Biuretic reaction.
- •2.2. Millon’s reaction.
- •2.4. Geller’s test.
- •3. Qualitative reaction to thyroxine.
- •4. Qualitative reactions to the 11-dehydro-17-oxykortikosteron (cortisone).
- •4.1. The reaction with phenylhydrazine sulfate.
- •4.2. The reaction with Fehling's reagent.
- •Test Questions
- •Laboratory work 6. Mineral and water and salt metabolism
- •1.1. Determination the pH of saliva.
- •1.2. Detection of phosphates in saliva.
- •2.1. Qualitative detection of chlorides in the urine.
- •2.2. Detection of calcium in the urine.
- •2.3. Detection of phosphates in the urine.
- •The composition of mixtures for the calibration curve
- •Test Questions
- •Laboratory work 7. Urine biochemistry
- •3.1. Qualitative detection and quantitative determination of protein in the urine.
- •3.1.1. The test by boiling in weak acid environment.
- •3.1.2. The test by boiling in an acid medium in the presence of saturated sodium chloride solution.
- •3.1.3. Geller’s test.
- •3.1.4. The test with sulfosalicylic acid.
- •3.1.5. Quantitative determination of protein in the urine by the method of dilution (Brandberg - Roberts - Stolnikov method).
- •Determination of protein in the urine using dilution method
- •3.2. Semi-quantitative method for determining glucose and ketone bodies in urine using test strips.
- •3.3. Detection of blood pigments in the urine by boiling with alkali (Geller’s test).
- •Test Questions
- •Laboratory 8. Blood biochemistry
- •1. Buffer properties of blood serum.
- •2. Quantitative determination of total protein in serum according to biuretic reaction.
- •The composition of mixtures for the ployying of the calibration curve
- •3. Determination of calcium in serum by the method of de Waard.
- •Test Questions
- •Laboratory work 9. Detection of bile pigments in urine
- •Test Questions
- •Laboratory work 10. Biochemistry of bone and connective tissue
- •1. Preparation of extracts of bone and teeth tissues.
- •Test Questions
- •Bibliography
- •Biochemistry
- •In Two Parts Part II
- •392008, Г. Тамбов, ул. Советская, 190г
Test questions
1. Give classification of lipids, specifying functions of each class of lipids in an organism.
2. Name structural components acting as hydrophobic and hydrophilic groups in lipids: phosphatidylethanolamine; sphingomyelin; cholesterol.
3. Name products formed during hydrolysis in intestine of the following compounds: 1-stearyl-2,3-dipalmityl-glycerol; 1-palmityl-2-oleyl-phosphatidylcholine.
4. What is the role of bile acids in digestion of lipids?
5. Give the sequence of reactions of triglycerides synthesis from fatty acids.
6. What stages are included by the process of β- oxidation of fatty acids? Where are these reactions localised?
7. During what process redused NADP necessary for the synthesis of higher fatty acids is formed?
8. In what organs cholesterol synthesis basically occurs?
9. Name the key enzyme of cholesterol synthesis.
10. Why hypercholesterolemia and not hypocholesterinemia more often occur?
11. How do we classify transport lipoproteins? Specify their functions.
12. How does the synthesis of unsaturated fatty acids occur?
13. Give the scheme of phospholipids breakdown under the influence of phospholipase.
14. What unsaturated acid is nesessary for the synthesis of eicosanoids?
15. What lipid metabolism violations are known to you?
16. Characterise the mechanism of atherosclerosis development.
2. Proteins metabolism
Protein metabolism has a special place. It provides reproduction and renewal of the body proteins, controls variety of chemical reactions in living organism. All other kinds of metabolism serve for the protein metabolism. Carbohydrate metabolism is mainly a source of carbon chains in amino acids biosynthesis. Fats metabolism supplies necessary energy. Nucleic acids metabolism provides storage and transfer of information about protein synthesis. Mineral metabolism promotes formation or disintegration of enzymatic systems by means of which protein synthesis occurs.
Protein metabolism is related to providing the body with vitamins and regulating the activity of the endocrine glands. For example, after the injection of thyroid gland hormones intensive degradation of tissue proteins is observed. Androgens and estrogens promote protein synthesis. Protein metabolism proceeds more intensively in child age, during active muscle work, pregnancy and lactation.
The main sources of proteins for humans are food of animal and vegetable origin. Protein content: soy (soya beans) - 35%, peas - 26%, meat, fish - 18-22%, potatoes - 1,5-2%, apples - 0,3-0,4%.
The intake of dietary protein is 100-120 g/day for an adult who is engaged in brainwork, 130-150 g/day are necessary for workers who are carrying out heavy physical activity.
The qualitative composition of protein nutrition is very important. Only 10 out of 20 necessary amino acids are synthesized in a human body. These are essential amino acids. The others 10 amino acids should be got with nutrition. Essential amino acids are valine, leucine, isoleucine, lysine, methionine, threonine, tryptophan, phenylalanine. Arginine and histidine are semi-essential, because adult organism can partially synthesize them. The absence or even lack of one essential amino acid can limit biosynthesis of all proteins in an organism.
There are biologically more valuable and less valuable proteins. For human the proteins of meat, milk, eggs are biologically more valuable, as their amino acid composition is closer to the amino acid composition of human body. The composition of proteins of wool, hair, feathers is also close to human body proteins, but they are not hydrolyzed by intestine proteinases and not used as nutrients.
Proteins are not stored, but as the end products of nitrogen metabolism they are excreted with urine.
Due to insufficient intake of proteins with meal proteins of liver, muscles, blood plasma (reserve proteins) degrade (about 25g/day). The formed amino acids are used for synthesis of necessary proteins, enzymes, hormones, and also as energy sources.
More than 95% of all nitrogen in an organism is nitrogen of amino acids (as part of proteins and free). Amino acid and protein metabolism can be judged by the state of the nitrogen balance. Nitrogen balance is the measure of nitrogen output subtracted from nitrogen input. Healthy adult with normal nutrition has nitrogen equilibrium. During the period of organism growth, as well as after convalescence from exhausting diseases nitrogen is deduced less, than it arrives, it is a positive nitrogen balance. Ageing, starving and during exhausting diseases an organism deduces more nitrogen than it gets, it is a negative nitrogen balance. A positive value is often found during periods of growth, tissue repair or pregnancy. This means that the intake of nitrogen into the body is greater than the loss of nitrogen from the body. A negative value can be associated with burns, ageing, starving and exhausting diseases. This means that the amount of nitrogen excreted from the body is greater than the amount of nitrogen ingested.