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lytic enzymes. Biochemistry of enzymes. Structure, properties and functions. Functions of enzymes in the cell

Faculty of Agriculture

Veterinary pharmacology

"Enzymes"

Sergeeva L.S.

Group SV-31

ENZYMES -biological catalysts, organic substances of protein nature, which are synthesized in cells and many times accelerate the reactions occurring in them, without undergoing chemical transformations. Enzymes are sometimes called enzymes.

All intracellular and extracellular metabolic processes are carried out in the body with the direct participation of enzymes. For the most part, enzymes are complex substances consisting of protein and prosthetic parts (apoenzyme). Apoenzymes are coenzymes (phosphorylated vitamins) and cofactors (BAS, macro-microelements)

The study of the chemical properties of enzymes and the reactions they catalyze is a special, very important area of ​​biochemistry - enzymology.

The structural features of enzymes necessary for their functioning are easily lost. So, when heated there is a rearrangement of the protein chain, accompanied by a loss of catalytic activity. Also important alkaline or acidic properties of the solution. Most enzymes work best in solutions , whose pH is close to 7, when the concentration of H + and OH - ions is approximately the same. This is due to the fact that the structure of protein molecules and, consequently, the activity of enzymes strongly depend on the concentration of hydrogen ions in the medium.

coenzymes and substrates. Many large molecular weight enzymes exhibit catalytic activity only in the presence of specific low molecular weight substances called coenzymes (or cofactors). The role of coenzymes is played by most vitamins and many minerals; that is why they must be ingested with food. A substance that is converted into the presence of an enzyme is called a substrate. Enzymes have an active site by which it attaches to the enzyme. active center is a unique combination of amino acid residues that provide direct interaction and specificity of the enzyme to the substrate. Each enzyme has one or more active sites to which the substrate binds. These centers are highly specific; "recognize" only "their" substrate or closely related compounds. In addition to the active center, the enzyme molecule has an allosteric center. When this center is connected to the substrate, the conformation of the enzyme molecule, including the active center, changes, which causes an increase or decrease in catalytic activity. The substrate joins the enzyme, which accelerates the breaking of some chemical bonds in its molecule and the creation of others; the resulting product is detached from the enzyme. This process is presented as follows:

The mechanism of action of enzymes.The rate of the enzymatic reaction depends on the concentration of the substrate[S]and the amount of enzyme present. These values ​​determine how many molecules of the enzyme will be connected to the substrate, and the rate of the reaction catalyzed by this enzyme depends on the content of the enzyme-substrate complex. The dependence of the rate (v) of the enzymatic transformation of the substrate on its concentration [S] is described by the Michaelis-Menten equation:

where K M is the Michaelis constant characterizing the activity of the enzyme, V is the maximum reaction rate at a given total concentration of the enzyme. It follows from this equation that at small [S], the reaction rate increases in proportion to the concentration of the substrate. However, with a sufficiently large increase in the latter, this proportionality disappears: the reaction rate ceases to depend on [S] - saturation occurs when all enzyme molecules are occupied by the substrate.

Enzymes perform many functions in the body. They catalyze a variety of synthesis reactions, including the formation of tissue proteins, fats, and carbohydrates. Entire enzyme systems are used to synthesize the vast array of chemical compounds found in complex organisms. This requires energy, and in all cases it comes from phosphorylated compounds such as ATP.

All enzymes formed in the body were classified into 6 classes depending on what reaction they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases.

Enzymes and digestion. Enzymes are essential participants in the digestion process. Only low molecular weight compounds can pass through the intestinal wall and enter the bloodstream, so food components must first be broken down into small molecules. This occurs during the enzymatic hydrolysis (breakdown) of proteins to amino acids, starch to sugars, fats to fatty acids and glycerol. The hydrolysis of proteins is catalyzed by the enzyme pepsin contained in the stomach. A number of highly effective digestive enzymes are secreted into the intestines by the pancreas. These are trypsin and chymotrypsin, which hydrolyze proteins; lipase, which breaks down fats; amylase catalyzes the breakdown of starch. Pepsin, trypsin and chymotrypsin are secreted in an inactive form, in the form of the so-called. zymogens (proenzymes), and become active only in the stomach and intestines. This explains why these enzymes do not destroy the cells of the pancreas and stomach. The walls of the stomach and intestines are protected from digestive enzymes and a layer of mucus. Several important digestive enzymes are secreted by cells in the small intestine.

Most of the energy stored in plant foods, such as grass or hay, is stored in cellulose, which is broken down by the enzyme cellulase. In the body of herbivores, this enzyme is not synthesized, and ruminants, such as cattle and sheep, can eat food containing cellulose only because cellulase is produced by microorganisms that inhabit the first section of the stomach - the rumen.

Enzymes and their preparations are very widely used in veterinary medicine not only as a means of improving digestion, but also as a means of auxiliary and independent prescription for many diseases. Synthetically, proteolytic enzymes were obtained:

    improving digestion(pepsin, chymotrypsin, abomin) in diseases of the gastrointestinal tract

    possessing fibrinolytic properties (fibrinolysin, streptolyase) are used for thrombosis and thrombophlebitis

    substances that reduce viscosity of hyaluronic acid(Lidase, Ronidase) is used for tendon contractures, scars after burns, operations, and hematomas. With reduced joint mobility after inflammation;

    lytic(antimicrobials)) lysosubtilin, lysozyme), lysing the walls of bacteria and causing their death

    The drugs used in purulent-necrotic processes (trypsin, collagenase) - iruksol, olasol.

    Enzyme preparations microbial origin mainly added to premixes and animal feed. Obtained from the cultivation of microbes and fungi. Under their influence, the digestibility of nutrients, especially plant foods, improves; the composition of the intestinal microflora is normalized, since some of them have an antimicrobial property; the growth of young animals is activated and some diseases of the gastrointestinal tract are prevented. According to the degree of purification, bacterial enzymes are divided into purified (alcohol and salting out) and technical (dried). Enzymes are obtained by deep or surface cultivation. Preparations: Amylorosin And Pectavamorin from the fungus aspergillus; Protosubtilin bacterial protease, acid protease from the fungus aspergillus.

    Lytic enzymes used in the treatment of animals with infectious diseases. These enzymes lyse components of the bacterial wall, which consists mainly of (heteroisomo)peptidoglycan. Lysis is carried out using the enzymes amylase, glycosidase, protease.

In gynecological practice, for the treatment of patients with follicular vestibulitis, endometritis, trichomoniasis, lysozyme. In infectious pathology, where the etiological factor is staphylococcus, an enzymatic preparation is used lysostatin, with mycotic lesions of the birth canal (candidomycosis, aspergillosis) is prescribed Kopran, Bolbit preparations of lower fungi. In the treatment of purulent-necrotic processes, proteolytic preparations are used. Profenzym, Imozin.

Lysosubtilin- powder, soluble in granules. Lytic activity is measured in units. used in the treatment of endometritis in cows. Dissolved in distilled water and injected into the uterus. For the prevention of diarrhea in calves, they are added to milk, colostrum.

Lysozyme - powder dissolved in water is administered orally with food and water. Used for fattening broilers, prescribed for complex therapy for bronchopneumonia, diarrhea, osteodystrophy.

Pepsinorm- enzyme-bacterial preparation. They produce both solution and powder. Normalizes digestion, eliminates dysbacteriosis, is used to treat diseases of the gastrointestinal tract of young animals.

    Enzymes used in purulent-necrotic processes.

Trypsin - obtained from the pancreatic gland of cattle. In powder or solution form. It is an endogenous proteolytic enzyme that cleaves peptide bonds in proteins. The application is based on the property of splitting necrotic tissues and fibrinous formations, thinning viscous exudates, blood clots. It is used intramuscularly in the treatment and prevention of bronchopneumonia in calves, in the form of aerosols for respiratory diseases to thin the exudate. Outwardly in the form of drops, lotions are used for burns, ulcers, purulent lesions, bedsores. Do not inject into a vein, bleeding cavities, malignant tumors.

Chymotrypsin- obtained from the pancreas of cattle, used as trypsin.

collagenase- from the pancreas of cattle, has the appearance of a porous mass. It has a proteolytic effect, carrying out the lysis of collagen fibers, promotes the melting of scabs and necrotic tissues. Applied topically for burns, frostbite, ulcers in order to accelerate the rejection of dead tissue

Ointment "Iruksol"

    Enzyme preparations that improve digestion .

Pepsin- powder soluble in water. The glands of the stomach produce an inactive form of pepsin - pepsinogen, which is converted in the stomach under the action of hydrochloric acid into the active form of pepsin. Acido-pepsin tablets are produced, consisting of 1 part of pepsin and 4 parts of hydrochloric betaine in the stomach, betaine is hydrolyzed with the release of hydrochloric acid and activates pepsinogen. It is prescribed for digestive disorders, achilia, hypo and anacid gastritis. Dyspepsia.

natural gastric juice transparent liquid of sour taste, with a specific smell. Obtained from dogs, horses with imaginary feeding according to Pavlov. Applied inside with hypofunction of the stomach, akhiliya.

Abomin- contains the amount of proteolytic enzymes, is used for various disorders of the digestive processes and lowering the level of acidity of gastric juice (gastritis, gastroenteritis, enterocolitis)

Pancreatin (Mezim) - obtained from the pancreatic gland of cattle. They produce powder, tablets, soluble in the intestine. The main enzymes: trypsin, amylase, lipase, splitting proteins, carbohydrates, fats. It is used for digestive disorders caused by hypofunction of the pancreas, with achilia, chronic pancreatitis, anacid gastritis, hypoacid enterocolitis. They are introduced into the feed and with water, an alkaline solution (soda) is added. At the same time, gastric juice is not used, hydrochloric acid and pepsidil are not administered.

Oraza- contains proteolytic and amylolytic enzymes, powder. It is not destroyed in the stomach, retains its catalytic activity in the intestine. It is used for digestive disorders associated with reduced function of the digestive glands. With anacid and hypoacid gastritis, with hepatocholecystitis, acute and chronic pancreatitis, gastric ulcer, colitis, accompanied by constipation.

    Various enzyme preparations

Lidaza - contains hyaluronidase. Obtained from the testes of cattle. Produce powder and lyophilized mass. Enter s / c, / m and inhalation in the form of aerosols. The substrate for hyaluronidase is hyaluronic acid, which is a mucopolysaccharide. It has a high viscosity and is a cementing compound in connective tissue. Hyaluronidase causes the breakdown of hyaluronic acid and reduces its viscosity while increasing tissue permeability and facilitating fluid circulation in the intercellular space. Apply with contractures of tendons, scars after burns, operations, with hematomas. Enter s / c with novocaine or under scar tissue.

Ronidase- indications for use are the same + joint stiffness after inflammation.

Cytochrome C- from the heart muscle of cattle, solution, tablets, soluble in the intestine. Refers to antihypoxic agents, used to improve intracellular respiration in neonatal asphyxia, chronic pneumonia, heart failure, coronary heart disease and other conditions accompanied by a violation of oxidative processes in the body, with increased loads to prevent tissue respiration failure.

    Enzyme inhibitors. Many inhibitors bind to the active site of the enzyme, the one with which the substrate interacts. In such inhibitors, the most important structural features are close to those of the substrate, and if both the substrate and the inhibitor are present in the reaction medium, they compete for binding to the enzyme; the higher the concentration of the substrate, the more successfully it competes with the inhibitor. Inhibitors of another type induce conformational changes in the enzyme molecule, which involve functionally important chemical groups.

Pantripin- from the pancreatic gland of cattle, powder, soluble in water. It has a polypeptide structure, has antiproteolytic activity against pancreatic enzymes (trypsin, chymotrypsin, kallikreia. The introduced pantrypin inhibits catalytically active enzymes formed in acute and chronic pancreatitis and other pathologies, in which the enzymes already in the gland itself acquire catalytic activity and digest it ( tumors, injuries, neoplasm infections).

Enzymes are a special type of proteins that nature has assigned the role of catalysts for various chemical processes.

This term is constantly heard, however, not everyone understands what an enzyme or enzyme is, what functions this substance performs, and how enzymes differ from enzymes and whether they differ at all. We'll find out all this now.

Without these substances, neither humans nor animals would be able to digest food. And for the first time, mankind resorted to the use of enzymes in everyday life more than 5 thousand years ago, when our ancestors learned to store milk in "dishes" from the stomachs of animals. Under such conditions, under the influence of rennet, it turned into cheese. And this is just one example of how an enzyme works as a catalyst that speeds up biological processes. Today, enzymes are indispensable in industry, they are important for the production of leather, textiles, alcohol and even concrete. These beneficial substances are also present in detergents and washing powders - they help remove stains at low temperatures.

Discovery history

Enzyme in Greek means "sourdough". And mankind owes the discovery of this substance to the Dutchman Jan Baptist Van Helmont, who lived in the 16th century. At one time he became very interested in alcoholic fermentation and during the study he found an unknown substance that accelerates this process. The Dutchman called it fermentum, which means fermentation. Then, almost three centuries later, the Frenchman Louis Pasteur, also observing fermentation processes, came to the conclusion that enzymes are nothing but the substances of a living cell. And after some time, the German Eduard Buchner extracted the enzyme from yeast and determined that this substance is not a living organism. He also gave him his name - "zimaza". A few years later, another German, Willy Kuehne, proposed to divide all protein catalysts into two groups: enzymes and enzymes. Moreover, he proposed to call the second term “sourdough”, the actions of which extend outside living organisms. And only 1897 put an end to all scientific disputes: it was decided to use both terms (enzyme and enzyme) as absolute synonyms.

Structure: a chain of thousands of amino acids

All enzymes are proteins, but not all proteins are enzymes. Like other proteins, enzymes are made up of . And interestingly, the creation of each enzyme takes from a hundred to a million amino acids strung like pearls on a string. But this thread is not even - it is usually bent hundreds of times. Thus, a three-dimensional structure unique for each enzyme is created. Meanwhile, the enzyme molecule is a relatively large formation, and only a small part of its structure, the so-called active center, is involved in biochemical reactions.

Each amino acid is connected to a specific type of chemical bond, and each enzyme has its own unique amino acid sequence. To create most of them, about 20 types are used. Even minor changes in the amino acid sequence can dramatically change the look and feel of an enzyme.

Biochemical properties

Although a huge number of reactions occur in nature with the participation of enzymes, they can all be divided into 6 categories. Accordingly, each of these six reactions proceeds under the influence of a certain type of enzyme.

Reactions involving enzymes:

  1. Oxidation and reduction.

The enzymes involved in these reactions are called oxidoreductases. As an example, remember how alcohol dehydrogenases convert primary alcohols to aldehyde.

  1. Group transfer reaction.

The enzymes responsible for these reactions are called transferases. They have the ability to move functional groups from one molecule to another. This happens, for example, when alanine aminotransferases move alpha-amino groups between alanine and aspartate. Transferases also move phosphate groups between ATP and other compounds, and create them from residues.

  1. Hydrolysis.

The hydrolases involved in the reaction are able to break single bonds by adding elements of water.

  1. Create or remove a double bond.

This type of reaction occurs in a non-hydrolytic way with the participation of lyase.

  1. Isomerization of functional groups.

In many chemical reactions, the position of the functional group changes within the molecule, but the molecule itself is made up of the same number and types of atoms as it was before the reaction began. In other words, the substrate and product of the reaction are isomers. This type of transformation is possible under the influence of isomerase enzymes.

  1. The formation of a single bond with the elimination of the element water.

Hydrolases break bonds by adding water elements to the molecule. Lyases carry out the reverse reaction, removing the aqueous part from the functional groups. Thus, a simple connection is created.

How they work in the body

Enzymes speed up almost all chemical reactions that occur in cells. They are vital for humans, facilitate digestion and speed up metabolism.

Some of these substances help break down molecules that are too large into smaller "chunks" that the body can digest. Others, on the contrary, bind small molecules. But enzymes, scientifically speaking, are highly selective. This means that each of these substances is capable of accelerating only a certain reaction. The molecules that enzymes work with are called substrates. The substrates, in turn, form a bond with a part of the enzyme called the active site.

There are two principles that explain the specifics of the interaction of enzymes and substrates. In the so-called "key-lock" model, the active site of the enzyme occupies the place of a strictly defined configuration in the substrate. According to another model, both participants in the reaction, the active site and the substrate, change their shapes in order to connect.

Whatever the principle of the interaction, the result is always the same - the reaction under the influence of the enzyme proceeds many times faster. As a result of this interaction, new molecules are “born”, which are then separated from the enzyme. And the catalyst substance continues to do its job, but with the participation of other particles.

Hyper- and hypoactivity

There are times when enzymes perform their functions with the wrong intensity. Excessive activity causes excessive reaction product formation and substrate deficiency. The result is poor health and serious illness. The cause of enzyme hyperactivity can be either a genetic disorder or an excess of vitamins or used in the reaction.

Enzyme hypoactivity can even cause death when, for example, enzymes do not remove toxins from the body or ATP deficiency occurs. The cause of this condition can also be mutated genes or, conversely, hypovitaminosis and a deficiency of other nutrients. In addition, lower body temperature similarly slows down the functioning of enzymes.

Catalyst and more

Today you can often hear about the benefits of enzymes. But what are these substances on which the performance of our body depends?

Enzymes are biological molecules whose life cycle is not determined by the boundaries of birth and death. They just work in the body until they dissolve. As a rule, this occurs under the influence of other enzymes.

In the course of a biochemical reaction, they do not become part of the final product. When the reaction is complete, the enzyme leaves the substrate. After that, the substance is ready to start working again, but on a different molecule. And so it goes on for as long as the body needs.

The uniqueness of enzymes is that each of them performs only one assigned function. A biological reaction occurs only when the enzyme finds the right substrate for it. This interaction can be compared with the principle of operation of a key and a lock - only correctly selected elements can work together. Another feature: they can work at low temperatures and moderate pH, and as catalysts they are more stable than any other chemicals.

Enzymes as catalysts speed up metabolic processes and other reactions.

As a rule, these processes consist of certain stages, each of which requires the work of a certain enzyme. Without this, the transformation or acceleration cycle cannot be completed.

Perhaps the most well-known of all the functions of enzymes is the role of a catalyst. This means that enzymes combine chemicals in such a way as to reduce the energy costs required to form a product more quickly. Without these substances, chemical reactions would proceed hundreds of times slower. But the abilities of enzymes do not end there. All living organisms contain the energy they need to continue living. Adenosine triphosphate, or ATP, is a kind of charged battery that supplies energy to cells. But the functioning of ATP is impossible without enzymes. And the main enzyme that produces ATP is synthase. For each glucose molecule that is converted into energy, synthase produces about 32-34 ATP molecules.

In addition, enzymes (lipase, amylase, protease) are actively used in medicine. In particular, they serve as a component of enzymatic preparations, such as Festal, Mezim, Panzinorm, Pancreatin, used to treat indigestion. But some enzymes can also affect the circulatory system (dissolve blood clots), accelerate the healing of purulent wounds. And even in anti-cancer therapy, they also resort to the help of enzymes.

Factors that determine the activity of enzymes

Since the enzyme is able to speed up reactions many times over, its activity is determined by the so-called turnover number. This term refers to the number of substrate molecules (reactive substances) that 1 enzyme molecule can transform in 1 minute. However, there are a number of factors that determine the rate of a reaction:

  1. substrate concentration.

Increasing the substrate concentration leads to an acceleration of the reaction. The more molecules of the active substance, the faster the reaction proceeds, since more active centers are involved. However, acceleration is possible only until all enzyme molecules are involved. After that, even increasing the concentration of the substrate will not accelerate the reaction.

  1. Temperature.

Usually, an increase in temperature leads to an acceleration of reactions. This rule works for most enzymatic reactions, but only as long as the temperature does not rise above 40 degrees Celsius. After this mark, the reaction rate, on the contrary, begins to decrease sharply. If the temperature drops below a critical point, the rate of enzymatic reactions will increase again. If the temperature continues to rise, the covalent bonds are broken and the catalytic activity of the enzyme is lost forever.

  1. Acidity.

The rate of enzymatic reactions is also affected by the pH value. Each enzyme has its own optimal level of acidity, at which the reaction proceeds most adequately. Changing the pH level affects the activity of the enzyme, and hence the rate of the reaction. If the change is too great, the substrate loses its ability to bind to the active nucleus, and the enzyme can no longer catalyze the reaction. With the restoration of the required pH level, the activity of the enzyme is also restored.

Enzymes present in the human body can be divided into 2 groups:

  • metabolic;
  • digestive.

Metabolic "work" to neutralize toxic substances, and also contribute to the production of energy and proteins. And, of course, they accelerate the biochemical processes in the body.

What the digestive organs are responsible for is clear from the name. But even here the principle of selectivity works: a certain type of enzyme affects only one type of food. Therefore, to improve digestion, you can resort to a little trick. If the body does not digest something from food well, then it is necessary to supplement the diet with a product containing an enzyme that can break down hard-to-digest food.

Food enzymes are catalysts that break down food to a state in which the body is able to absorb useful substances from them. Digestive enzymes come in several types. In the human body, different types of enzymes are found in different parts of the digestive tract.

Oral cavity

At this stage, alpha-amylase acts on the food. It breaks down carbohydrates, starches and glucose found in potatoes, fruits, vegetables and other foods.

Stomach

Here, pepsin breaks down proteins into peptides, and gelatinase breaks down the gelatin and collagen found in meat.

Pancreas

At this stage, "work":

  • trypsin - responsible for the breakdown of proteins;
  • alpha-chymotrypsin - helps the absorption of proteins;
  • elastase - break down certain types of proteins;
  • nucleases - help break down nucleic acids;
  • steapsin - promotes the absorption of fatty foods;
  • amylase - responsible for the absorption of starches;
  • lipase - breaks down fats (lipids) found in dairy products, nuts, oils, and meats.

Small intestine

Over food particles "conjure":

  • peptidases - break down peptide compounds to the level of amino acids;
  • sucrase - helps to absorb complex sugars and starches;
  • maltase - breaks down disaccharides to the state of monosaccharides (malt sugar);
  • lactase - breaks down lactose (glucose found in dairy products);
  • lipase - promotes the absorption of triglycerides, fatty acids;
  • erepsin - affects proteins;
  • isomaltase - "works" with maltose and isomaltose.

Colon

Here the functions of enzymes are performed:

  • coli - responsible for digestion;
  • lactobacilli - affect lactose and some other carbohydrates.

In addition to these enzymes, there are also:

  • diastase - digests vegetable starch;
  • invertase - breaks down sucrose (table sugar);
  • glucoamylase - converts to glucose;
  • alpha-galactosidase - promotes the digestion of beans, seeds, soy products, root vegetables and leafy vegetables;
  • bromelain - an enzyme derived from, promotes the breakdown of different types of proteins, is effective at different levels of acidity of the environment, and has anti-inflammatory properties;
  • papain, an enzyme isolated from raw papaya, promotes the breakdown of small and large proteins, and is effective over a wide range of substrates and acidity.
  • cellulase - breaks down cellulose, plant fibers (not found in the human body);
  • endoprotease - cleaves peptide bonds;
  • ox bile extract - an enzyme of animal origin, stimulates intestinal motility;
  • pancreatin - an enzyme of animal origin, accelerates the digestion of proteins;
  • pancrelipase - an animal enzyme that promotes the absorption

    Fermented foods are a near-perfect source of beneficial bacteria needed for proper digestion. And while pharmacy probiotics "work" only in the upper digestive system and often do not reach the intestines, the effect of enzymatic products is felt throughout the gastrointestinal tract.

    For example, apricots contain a mixture of beneficial enzymes, including invertase, which is responsible for the breakdown of glucose and promotes rapid energy release.

    A natural source of lipase (promotes faster digestion of lipids) can serve. In the body, this substance is produced by the pancreas. But in order to make life easier for this body, you can treat yourself, for example, to a salad with avocado - tasty and healthy.

    In addition to being perhaps the most famous source, it also supplies amylase and maltase to the body. Amylase is also found in bread and cereals. Maltase aids in the breakdown of maltose, the so-called malt sugar, which is abundant in beer and corn syrup.

    Another exotic fruit - pineapple contains a whole range of enzymes, including bromelain. And it, according to some studies, also has anti-cancer and anti-inflammatory properties.

    Extremophiles and industry

    Extremophiles are substances that can survive in extreme conditions.

    Living organisms, as well as the enzymes that enable them to function, have been found in geysers where the temperature is close to the boiling point, and deep in ice, as well as in conditions of extreme salinity (Death Valley in the USA). In addition, scientists have found enzymes for which the pH level, as it turned out, is also not a fundamental requirement for effective work. Researchers are studying extremophile enzymes with particular interest as substances that can be widely used in industry. Although even today enzymes have already found their application in the industry as biologically and environmentally friendly substances. The use of enzymes is resorted to in the food industry, cosmetology, and the production of household chemicals.

    Izvozchikova Nina Vladislavovna

    Speciality: infectious disease specialist, gastroenterologist, pulmonologist.

    General experience: 35 years .

    Education:1975-1982, 1MMI, San-Gig, highest qualification, infectious diseases doctor.

    Science degree: doctor of the highest category, candidate of medical sciences.