- •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. Describe the chemical composition of the brain.
2. What are the peculiarities of metabolism in nervous tissue?
3. List the functions of glutamate in the nervous tissue.
4. What is the role of mediators in the transmission of nerve impulses?
5. What are the differences in the functioning of cholinergic and adrenergic synapses?
6. Give the examples of compounds that affect the synaptic transmission of nervous impulses.
7. What biochemical changes may occur in the nervous tissue in mental disordes?
9. Biochemistry of muscle tissue
Muscles make up 40-50% of body weight.
There are three types of muscle:
Striated skeletal muscle (contracted voluntarily);
Striated cardiac muscle (contracted involuntarily);
The smooth muscles (blood vessels, intestines, uterus) (contracted involuntarily).
Striated muscle consists of numerous elongated fibers.
Muscle fiber is a multinucleated cell, covered by elastic coat – sarcolemma. The muscle fiber includes motor nerves, which transmit nerve impulses to it, causing contraction. There are filamentous formations – myofibrils – in the semiliquid sarcoplasm along the length of the fibers. Sarcomere is a repeated element of myofibrils, limited by Z-line (Fig. 9). In the middle of the sarcomere there is the A disk (dark in phase-contrast microscope); in the centre of which there is M-line, visible by electron microscopy. H-zone occupies the central part of the A-disk. I-disks are light in a phase-contrast microscope, and each is divided into equal halves of Z-line. In the A-discs there are thick myosin and thin actin filaments. Thin filaments begin at Z-lines, and then they pass through the I-disk and are interrupted in the region of H-zone. Electron microscopy showed that thick filaments are arranged in a hexagon shape and pass through the A-disk. The thin filaments are between the thick ones. During the contraction of muscle, the I-discs virtually disappear, and the region of overlap between thin and thick filaments increases.
Fig. 9. The structure of the muscle fiber
Sarcoplasmic reticulum is the intracellular membrane system of interconnected flattened vesicles and tubules; it surrounds the sarcomeres of myofibrils. There are proteins on the inside membrane which are capable of binding calcium ions.
9.1. Chemical composition of muscle tissue
The muscle tissue consists of 72-80% of water; 20-28% is dry residue (proteins, carbohydrates, lipids, non-protein nitrogen-containing substances, etc.).
Muscle proteins are sarcoplasmic (35% of muscle protein), myofibrillar (45%) and stromal proteins (20%).
Sarcoplasmic proteins are soluble in salt solutions with low ionic strength. It is a mixture of proteins with properties of globulins; proteins with enzymatic activity (glycolytic enzymes); myoglobin; enzymes of tissue respiration, oxidative phosphorylation, nitrogen and lipid metabolism; parvalbumins linking calcium ions.
Myofibrillar proteins are soluble in salt solutions with high ionic strength and are closely associated with the contractile function of muscles. They are myosin, actin, actomyosin, regulatory proteins (tropomyosin, troponin, α- and β-actinin).
Myosin is 50% dry mass of myofibrils. It is elongated molecule which consists of two subunits: two heavy polypeptide chains (Mr = 210 000) and a few of light (Mr = 20,000).
Myosin heavy chains are long a-helix. It is the "tail" of the molecule. The end of the heavy chain (together with the light one) makes up the "head" of the molecule (globule), which is combined with actin. Light chains of "head" of the myosin molecules are involved in the manifestation of the ATPase activity of myosin. Myosin is inhibited by Mg2+ ions and is not inhibited by high concentrations of ATP. Sarcomere thick filaments are the connections of many myosin molecules definitely oriented in the space.
Actin (20% dry mass of myofibrils) is presented in two forms: globular (G-actin) and fibrillar (F-actin). G-actin is polypeptide chain (globule). Polymer of G-actin is F-actin which molecule is similar to the two strands of beads twisted around one another.
Actomyosin is a complex of myosin with F-actin. It has ATPase activity. Actomyosin ATPase is activated by magnesium cations, and inhibited by high concentrations of ATP.
Tropomyosin consists of two α-helices and has the form of stick (4-7% of the proteins of myofibrils).
Troponin (Tn) – is a globular protein (2% of the proteins of myofibrils), has subunit which inhibits ATPase activity (Tn-I), calcium-binding (Tn-C) and tropomyosin-binding (Tn-T) subunits.
Troponin complex with tropomyosin is called native tropomyosin. It attaches to actin and allows sensitivity of actomyosin to calcium ions.
Stroma proteins are collagen and elastin.
Non-protein nitrogen-containing substances are nucleotides, adeninylic primarily (ATP, ADP, AMP). Creatine and creatine phosphate are involved in processes of muscle contraction. Creatine is synthesized in the liver, with bloodstream is transferred to the muscle tissue and there it is phosphorylated. Creatine phosphate is formed. Carnosine and anserin are imidazole containing dipeptides that are specific to skeletal muscles of vertebrates. They increase the amplitude of muscle contraction during fatigue. Amino acids are glutamic acid and glutamine.
Phosphoglycerides – phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, and others are part of the cell membranes of muscle tissue, they are substrates of tissue respiration.
Products of nitrogen metabolism – urea, uric acid, adenine, guanine, xanthine, hypoxanthine – occur in the muscles in small quantities.
Nitrogen-free substances.
The main representative is glycogen. In muscle tissue lactic and pyruvic acid are produced during the metabolism of glucose and amino acids. There are also triglycerides and cholesterol.
Inorganic substances: cations of potassium (in muscle fibers), of sodium (intercellular substance), magnesium, calcium and iron. There are microelements (cobalt, aluminum, nickel, zinc, etc.).
The chemical composition of the cardiac muscle and smooth muscle
Compared with the skeletal muscles they contain less myofibrillar proteins, more stroma proteins and mioalbumin in the sarcoplasm. ATP content in cardiac muscle is higher than in smooth muscle, and lower than in skeletal. The myocardium contains many phosphoglycerides, during the oxidation of which most of the energy for its contraction is formed. Trace amounts of carnosine and anserine are detected.
