- •Introduction into biochemistry
- •General properties
- •Classification of proteins
- •Simple Proteins – representatives, properties and role
- •Globulins [g]
- •Histones (h) h are basic non value proteins. Localized in nucleus with mol. Mass (mm) 10000-20000 d. They contain of 30% diaminomonocarboxylic acids and have positive charge. Their iep is equal 10.
- •Table 1 “The properties of globular simple proteins”
- •Conjugated proteins
- •Table 2 Composition of the free (transport) lipoproteins in plasma of human
- •True gp Proteoglycans
- •Table 3 Chemical nature of glycosaminoglycans
- •Nucleoproteins (np)
- •Mononucleotides
- •Table 4 The composition and names of nucleosides, nucleotides and their phosphoric derivatives
- •Structure of dna Primary st. Of dna is a spirally one polynucleotides chain (pnc), the disposition of nucleotides in which determine all hereditary properties of organism.
- •Structure of rna
- •Enzymes
- •Mechanism of enzyme action
- •Factors influencing on enzyme activity
- •Enzyme inhibition
- •Classification of enzymes
- •III. Hydrolases
- •Bioenergetics
- •Table 6 Redox potential (rp)
- •Inhibition of oxidative phosphorylation.
- •The types of oxidation
- •Peroxidase’s type
- •Vitamins
- •Vitamin b12
- •Ascorbic acid (vitamin c)
- •Rutin, vitamin p (permeability) – bioflavonoids, capillaris’s strengthening
- •Fat soluble vitamins
- •Deficiency diseases
- •Vitamin k
- •Carbohydrates metabolism. Digestion and absorption of carbohydrates. Intermediate metabolism of carbohydrates
- •Carbohydrates metabolism. Intermediate and final stages of carbohydrates metabolism
- •Lipids of food, their importance, digestion, absorption. Micelles and chylomicrons. The role of intestinal wall, liver, lungs and adipose tissue in lipid metabolism
- •Lipids metabolism. Lipoproteins, their composition and role. The pathways of usage of glycerol and free fatty acids in cells
- •“Pathologic chemistry of lipid’s metabolism”
- •The intermediate Metabolism of Simple Proteins (part 1): the conversion of amino acids in tissues. The formation and usage of Creatine. The decarboxylation of amino acids, the role of biogenic amines
- •Simple proteins metabolism. The pathways of formation and detoxification of ammonia
- •Conjugated proteins metabolism
- •Biochemistry of liver
- •Classification of hormones
- •General properties of hormones
- •Hormones of epiphysis Melatonin
- •Hypothalamic hormones
- •Vasopressin (antidiuretic hormone)
- •Oxytocin
- •Hormones of hypophysis
- •Hormones of pancreas
- •Hormones of adrenal glands
- •Sexual hormones are formed in gonads.
- •Estrogens
- •If the pregnancy beginns so development of embryo occurs; if the pregnancy doesn’t occur so degeneration of yellow body proceeds and mensis beginns again Androgens
- •Biochemistry of blood plasma
- •Table 10 a main biochemical indices in the blood plasma (serum)
- •Functions and diagnostic importance of some fractions of proteins Table 11 Biologic and clinic importance of blood serum proteins
- •Blood clotting system
- •Blood dissolution system
- •Complement system
- •Inorganic constituents of blood plasma. Water-mineral metabolism. Acidosis and alkalosis
- •Acidosis and alkalosis Table 12 Acidosis and alkalosis
- •Water metabolism
- •Biochemistry of erythrocytes
- •Metabolism in erythrocytes
- •The physiological and pathological derivatives of hemoglobin and their spectra of taking up
- •Biochemistry of white blood cells
- •Biochemistry of kidneys
- •Normal and pathologic constituents of urine. Urine analysis – its clinical significance Composition of normal urine
- •Physical examination
- •I. Volume
- •The term polyuria implies an increased volume of urine
- •II. Colour
- •III. Specific Gravity
- •Clinical significance
- •IV. Acidity and pH
- •Clinical Significance
- •V. Odor
- •Causes of abnormal odor
- •VI. Turbidity
- •Types of turbidities
- •Inorganic constituents
- •Chlorides
- •Clinical significance
- •Organic constituents
- •Clinical significance
- •II. Ammonia
- •Clinical significance
- •Increase
- •Uric acid
- •Clinical significance
- •Clinical aspect
- •Creatinine and creatine
- •Oxalic Acid
- •Clinical significance
- •Aminoacids
- •Aminoacidurias
- •Abnormal constituents
- •Proteins
- •Proteinuria
Factors influencing on enzyme activity
Effect of temperature
The optimum of temperature is that temperature at which the activity of enzyme is maximal. For most enzymes optimal temperature is within the range from +35C to +45C. if the temperature is below than optimal one so that is called reversible innactivation of enzymes. In this case the increase of temperature to optimal one leads to the reactivation of enzymes. If the temperature is above than optimal one so that is called irreversible innactivation. In this case the increase of temperature above optimal one leads to the denaturation of enzymes and if decrease the temperature reactivation of enzymes isn’t observed.
The effect of pH on enzyme activity
The pH influences on the charge of active site of enzyme. The function of enzyme depends on the charge of active site. Optimal pH is pH of environment at which the activity of enzymes is maximal.
For most enzymes the optimal pH is within the range 4-7 (e.g. alfa-amylase has opt.pH 6.8). But there are exception. For example, enzyme pepsin has optimal pH 1.5-2.0; trypsin – 8.0-9.0.
The effect of enzyme concentration
Increase of enzyme concentration increases the enzymic activity (directly proportional relationship)
The effect of substrate concentration
The activity of enzymes is directly proportional to the substrate concentration. However, this is true only for a certain concentration after which the increase of its does not further increase the velocity of reaction. This phenomenon is named saturating concentration, i.e. all active sites are occupied by substrates and reaction doesn’t occur.
The influence of effectors
The effectors are divided into 2 groups: activators and inhibitors. Both of these groups have specific and non-specific representatives. For example, HCl (hydrochloric acid) is a specific activator for pepsin; ions of chlorine are specific activators for alfa-amylase; bile acids are specific activators for lipase of pancreas. Non-specific activators can activate many enzymes, e.g. ions of Mg are non-specific activators for phosphatases and kinases. Specific inhibitors are end-peptides of proenzymes. For example, pepsinogen is proenzyme (precursor of enzyme pepsin). It is activated by splitting off end-polypeptide under action of HCl. Such way is characteristically for most hydrolases of gaster and pancreas. For example, trypsinogen is activated by entherokinase (entheropeptidase) which splits off hexapeptide from its and trypsin is formed.
Non-specific inhibitors cause denaturation of enzyme, for example salts of heavy metals (copper sulfate etc).
Enzyme inhibition
There are competitive and non-competitive inhibition of enzymes. Beside of these 2 types of inhibition there are allosteric activation and inhibition of enzymes.
Competitive inhibition
This phenomenon occurs when inhibitor has structural resemblance with substrate. In this case inhibitor and substrate compete for binding with active site of enzyme. If the quantity of inhibitors more than substrate and complex enzyme-inhibitor is formed. For example, enzyme sucinate dehydrogenase. Its substrate is succinic acid and competitive inhibitors are malonic and oxaloacetic acids.
Enzyme glucose-6-phasphatase catalyzes the dephosphorylation of glucose-6-phosphate to glucose and phosphoric acid. glucose is competitive inhibitor. This is example of inhibition by products of reaction
Non-competitive inhibition
This inhibition is observed when there isn’t structural resemblance between inhibitor and substrate. Complex inhibitor-substrate-enzyme is formed due to binding of inhibitor to catalytic part of active site. For example, enzyme cytochrome oxydase. Its substrate is oxygen and non-competitive inhibitor is cyanic acid or its salts (cyanides).
Allosteric regulation of enzymic activity
Some of enzymes with quaternary structure have allosteric center beside of active one. Allosteric center usually occurs near active site of enzyme. Modification of allosteric center is transmitted to active center and activity of enzyme is activated or inhibited in depend of action of allosteric activator or inhibitor. For example, adenylyl cyclase (or guanylyl cyclase) are enzymes with allosteric types of regulation.