- •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
11. Blood biochemistry
The main functions of the blood are related to the fact that it is liquid movable tissue that moves through the blood vessels. The blood serves as a transport and communication tools for integration of metabolism of different organs. The main functions of blood include:
- respiratory function (transfer of O2 from the lungs to the tissues and CO2 from the tissues to the lungs);
- trophic function (transfer products of digestion from the intestine to different organs: the glucose and ketone bodies from the liver to the muscle, fat from the liver to adipose tissue, lactic acid from muscle to the liver, fatty acids from adipose tissue to different organs, etc.) ;
- excretory function (urea transport from the liver to the kidneys, bilirubin from different tissues to the liver, etc.);
- communicative (regulatory) function (the transfer of hormones and other regulatory agents to target organs).
Other functions of blood: protective, performed by antibodies and phagocytic leukocytes; involvement in the regulation of water-salt and acid-base balance; regulation of body temperature by heat exchange between the tissues and blood moving are also related with the movement of blood.
The total amount of blood in an adult is about 5 liters (about 7% of body weight). It consists of a liquid portion and formed elements: erythrocytes, leucocytes and platelets. After sells sedimentation by centrifugation, the light-transparent liquid remains. It is blood plasma. Plasma protein fibrinogen after keeping for some time becomes insoluble fibrin, which forms a clot. Fluid which is squeezed out of the bunch is the blood serum. The serum differs from the plasma in the way that it does not contain protein fibrinogen.
The plasma composition is a kind of mirror of metabolism, because changes in the concentration of metabolites in cells, even if they occur in individual organs, are reflected in the concentrations of these metabolites in the blood.
Blood plasma is approximately 10% aqueous solution of organic and mineral substances. The concentration of protein is about 7%, mineral salts, about 1%, the rest is various non-protein organic compounds: urea, bilirubin, indican, creatine, creatinine, uric acid, glucose, fructose, lactic acid, pyruvic acid, etc.
Plasma proteins are represented by five fractions: albumins, α1-globulins, α2-globulins, β-globulins and -globulins. Each of these fractions is a mixture of different proteins. The most homogeneous is albumin fraction. -globulin fraction contains primarily antibodies (immunoglobulins). Other fractions are heterogeneous. Most of the proteins in plasma are synthesized in the liver.
The fraction of albumin is more than half (55-60% or 40-50 g / l) of the blood plasma proteins. Albumins transport of many biologically active substances (hormones, fatty acids in the mobilization of fats from fat depots). They can bind with cholesterol and bile pigments. A significant portion of calcium in serum is also bound with albumins. Albumins play an important role in maintaining the oncotic pressure of blood. When the concentration of albumin in serum is less than 30 g/l it causes significant changes in oncotic pressure of blood that leads to edema. The concentration of albumin in the blood can decrease because of its excretion in the urine in kidney diseases (albuminuria). The human liver synthesizes and secretes into the blood up to 15 g of albumin per day. In some diseases of the liver (cirrhosis), albumin synthesis is disturbed. These states are also characterized by edema.
Globulins are presented by two fractions - euglobulins and pseudo-globulins. Euglobulin fraction consists mainly of -globulins, and fraction of pseudo-globulins consists of α-, β- and -globulins. Most of the antibodies found in the fraction of -globulins. Immunoglobulins, or antibodies are synthesized by β-lymphocytes or by plasma cells formed from them. In a number of pathological conditions hyperproteinemia can occur due to increasing levels of -globulins: for example, as a result of infection.
In many diseases proportion of individual protein fractions of blood plasma is changed, although the total protein content in the blood serum remains within normal limits. This condition is called dysproteinemia.