In the blood, the five main fractions of proteins. Plasma proteins and their functions are the most important plasma proteins and their functions.

Blood plasma proteins

There are more than 200 species of proteins in the blood plasma, which make up 7% of the plasma volume. Blood plasma proteins are synthesized mainly in the liver and macrophages, as well as in the endothelium of vessels, in the intestines, lymphocytes, kidneys, endocrine glands. Blood plasma proteins of liver, kidneys, muscles, etc. are destroyed. The blood plasma proteins range from several hours to several weeks.

In blood plasma, proteins perform the following functions:

  1. Create oncotic pressure. It is necessary for retention of water in blood river.
  2. Participate in blood clotting.
  3. Form the buffer system (protein buffer).
  4. Transported in the blood of water-soluble substances (lipids, metals 2 or more valence).
  5. Participate in immune processes.
  6. Forms a reserve of amino acids, which is used, for example, with protein starvation.
  7. some reactions (proteins-enzymes) catalyze.
  8. The blood viscosity is determined, affect hemodynamics.
  9. Participate in inflammation reactions.

The structure of blood plasma proteins

In the structure of blood plasma proteins are globular, they are divided into simple (albumin) and complex.

Among the complex, lipoproteins (LPONP, LPLP, LDL, HDP, HM), glycoproteins (almost all plasma proteins) and metalloproteins (transferer, cerroplasmin) can be distinguished.

The total number of protein The blood plasma is normally 70-90 (60-80) g / l, it is determined using a buret reaction. The amount of total protein in the blood has a diagnostic value.

Increasing the total amount of protein in blood plasma is called hyperproteinemia decline - hypoproteinemia . Hyperproteinemia occurs during dehydration (relative), injuries, burns, myelomic disease (absolute). Hypoproteinemia occurs when the edema (relative), starvation, liver pathology, kidneys, blood loss (absolute).

In addition to the total content of proteins in the blood plasma, the content of individual groups of proteins or even individual proteins determine the content of individual proteins. For this, they are separated by electro-electroform.

Electrophoresis - This is a method in which substances with different charges and mass are separated in a constant electric field. Electrophoresis is carried out on various media, while getting miscellaneous number fractions. In electrophoresis on paper, blood plasma proteins are given 5 fractions: albumin, α 1 -Гlobulins, α 2 -Гlobulins, β-globulins and γ-globulines. In electrophoresis, 7-8 fractions are obtained on the agar gel, on the starch gel - 16-17 fractions. Most of the whole fractions - more than 30, gives immunoelectrophoresis.

Plasma proteins can also be divided by planting with neutral salts of alkali and alkaline earth metals (3 fractions: albumin, globulins and fibrinogen) or precipitation in alcohol solution.

Dencilogram Belkov

serum blood

Electhororegram protein

serum Blood (10 patients)

The feasibility of separation of proteins on the fraction is related to the fact that the protein fractions of blood plasma differ among themselves the protein predominance in them, with certain functions, a place of synthesis or destruction.

Violation of the ratio of protein factions of blood plasma is called disproteinemia . Dispretinemia detection has a diagnostic value.

Fractions of blood plasma proteins

I.. Albumin

The main protein of this fraction is albumin.

Albumen . A simple protein of 585 acres with a mass of 69kd has 17 disulfide bridges, many dicarboxylic ac, has high hydrophobicity. Albumin has polymorphism. It is synthesized in the liver (12 g / day), is disposed of by the kidneys, enterocytes, etc. tissues. T½ \u003d 20 days. 60% of albumines are in the intercellular substance, 40% - in the bloodstream. In the plasma of albumin 40-50g / l, they constitute 60% of all blood plasma proteins. Functions: Maintaining oncotic pressure (contribution 80%), transport of free fatty acids, bilirubin, grained acids, steroid and thyroid hormones, xs, drugs, inorganic ions (Cu 2+, CA 2+, Zn 2+ ) is a source of amino acids.

TransTaretin (Prehale) . Tetramer. Plasma 0.25g / l. Spicy phase protein (5 group). Transports thyroid hormones and retinol binding protein. Reduced when fasting.

Disproteinemia of the albumin fraction is implemented mainly due to hypoalbuminemia.

Cause of hypoalbummia It is a decrease in the synthesis of albumin during liver failure (cirrhosis), while increasing the permeability of capillaries, with the activation of catabolism due to burns, sepsis, tumors, with the loss of albumin with urine (nephrotic syndrome), during starvation.

Hypoalbuminemia causes Tissue swelling, renal blood flow reduction, activation of RAAS, water delay in the body and strengthening tissue edema. A sharp outflow of fluid in tissue leads to a decrease in blood pressure and can cause shock.

Globulins.Online lipoproteins and glycoproteins.

II.. α 1 -Globulins

α 1 -Antrippsin - Glycoprotein, synthesized by the liver. Plasma 2.5g / l. Spicy phase protein (2 group). An important inhibitor of proteases, including elastas neutrophils, which destroy Elastin Alveol Light and liver. α 1 -anttripsin also inhibits skin collagenase, chymotrypsin, fungi and leukocyte protease. With a deficiency of α 1 -anttripsin, emphysema of lungs and hepatitis, leading to the liver cirrhosis, may occur.

Sour α 1 - Glycoprotein , synthesized liver. Plasma 1 g / l. Spicy phase protein (2 group). Transports progesterone and accompanying hormones.

LDP. Synthesized in the liver. Plasma 0.35 g / l. Transport surplus Xc from tissues to the liver, ensure the exchange of other LPs.

Prothrombin - glycoproteide containing about 12% of carbohydrates; The protein part of the molecule is represented by one polypeptide chain; Molecular weight about 70000d. Plasma 0.1 g / l. Protrombin is the predecessor of the thrombin enzyme that stimulates the formation of a thrombus. Biosynthesis occurs in the liver and is regulated by vitamin K formed by intestinal flora. With its lack of vitamin to the level of prothrombin in the blood, it falls, which can lead to bleeding (early children's hemorrhage, obtuctive jaundice, some liver diseases).

Transcortin - Glycoprotein, synthesized in the liver, weight of 55700d, ½ \u003d 5 days. Transfers cortisol, corticosterone, progesterone, 17-alpha hydroxyprogesterone and, to a lesser extent, testosterone. Plasma 0.03 g / l. The concentration in the blood is sensitive to exogenous estrogen and depends on their dose.

Tyroxins binding globulin (TBG. ) - it is synthesized in the liver. Molecular weight of 57 kDa. Plasma 0.02 g / l. T½ \u003d 5 days. It is the main conveyor of thyroid hormones in the blood (transports 75% thyroxine and 85% triiodothyronine).

Disproteinemia Due to the α 1 -Гlobulin fraction is implemented mainly due to: 1). Reducing the synthesis α 1 -anttripsin. 2). Loss of proteins of this fraction with urine with nephrotic syndrome. 3). Enhance the proteins of the acute phase during the period of inflammation.

III. α 2 -Globulins

α 2 -Makroglobulin Very large protein (725 kDa), is synthesized in the liver. Spicy phase protein (4 group). Plasma 2.6 g / l. The main inhibitor sets the plasma proteinase classes, regulates blood coagulation, fibrinolysis, cyinogenesis, immune responses. The level α 2 -machroglobulin in plasma decreases in the acute phase of pancreatitis and prostate carcinoma, increases as a result of hormonal effect (estrogens).

Gaptoglobin - Glycoprotein, synthesized in the liver. Plasma 1 g / l. Spicy phase protein (2 group). Hemoglobin binds to the formation of a complex with peroxidase activity, prevents the loss of iron from the body. Haptoglobin effectively inhibits the Catence C, B and L, can participate in the disposal of some pathogenic bacteria.

Vitamin D binding protein (BSB) (weight 70kd). Plasma 0.4 g / l. Provides transport of vitamin A in plasma and prevents its excretion with urine.

Ceruloplasmin - The main copper-containing plasma protein (contains 95% copper in plasma) with a mass of 150kd, is synthesized in the liver. Plasma 0.35 g / l. T½ \u003d 6 days. Ceruloplasmin has pronounced oxidase activity; limits the release of iron, activates oxidation ascorbic acid, norepinephrine, serotonin and sulfhydrylic compounds, inactivates the active forms of oxygen, preventing the floor.

Ceruloplasmin - spicy phase protein (3 group). It rises in patients with infectious diseases, cirrhosis of the liver, hepatitis, myocardial infarction, systemic diseases, lymphogranulomatosis, with malignant neoplasms various localization (lung cancer, breast, cervical, gastrointestinal tract).

Wilson's disease is Konovalova. The insufficiency of ceruloplasmin occurs when it is violated its synthesis in the liver. With a shortage of ceruloplasminCu 2+ It leaves blood, is removed with urine or accumulates in tissues (for example, in the central nervous system, cornea).

Antrombin III . Plasma 0.3 g / l. Inhibitor of plasma proteases.

Retinol binding protein It is synthesized in the liver. Plasma 0.04 g / l. Rechanges Retinol, provides its transport and prevents decay. Function in the complex with transstaretin. Retinol binding protein fixes excess vitamin A, which prevents the membranolytic effect of high doses of vitamin.

Disproteinemia Due to the α 2-Gobulin fraction, it may occur during inflammation, because In this fraction, proteins of the acute phase are contained.

IV. β-globulins

LPONP - formed in the liver. Transportation TG, xs.

LPPP - formed in blood from LPONP. Transportation TG, xs.

LDL. - formed in blood from LPLP. Plasma 3.5 g / l. Transport surplus Xc from peripheral organs into the liver.

Transfirin - Glycoprotein, synthesized by the liver. Plasma 3 g / l. T½ \u003d 8 days. The main conveyor of iron in the plasma, 1 transferlic molecule binds 2 Fe 3+, and 1g transferrin, respectively, about 1.25 mg of iron. With a decrease in iron concentration, transferen synthesis increases. Spicy phase protein (5 group). Reduced during liver failure.

Fibrinogen Glycoprotein, synthesized in the liver. Molecular weight of 340kd. Plasma 3 g / l. T½ \u003d 100 hours. Factor I of blood turning, is capable of transforming into fibrin under the action of thrombin. It is a source of fibrinopetides with anti-inflammatory activity. Spicy phase protein (2 group). The content of fibrinogen increases with inflammatory processes And tissue necrosis. Reduced with DVS syndrome, liver failure. The fibrinogen of the main plasma protein affecting the SE value (with an increase in fibrinogen concentration of the erythrocyte sedimentation rate increases).

C-reactive protein It is synthesized mainly in hepatocytes, its synthesis is initiated by antigens, immune complexes, bacteria, mushrooms, during injury (4-6 hours after damage). It can be synthesized by endotheliocytes of arteries. In plasma<0,01 г/л. Белок острой фазы (1 группа). Способен связывать микроорганизмы, токсины, частицы поврежденных тканей, препятствуя тем самым их распространению. Эти комплексы активируют комплемент по классическому пути, стимулируя процессы фагоцитоза и элиминации вредных продуктов. С-реактивный белок может взаимодействовать с Т-лимфоцитами, фагоцитами и тромбоцитами, регулируя их функции в условиях воспаления. Обладает антигепариновой активностью, при повышении концентрации ингибирует агрегацию тромбоцитов. СРБ - это маркер скорости прогрессирования атеросклероза. Определяют для диагностики миокардитов, воспалительных заболеваний клапанов сердца, воспалительные заболевания различных органов.

Disproteinemia Due to the β-globuline fraction may occur at 1). some dlyppostinemia; 2). inflammation, because In this fraction, the proteins of the acute phase are contained; 3). With a violation of the coagulation system of blood.

V.. γ-globulins

Synthesized functionally active in lymphocytes (plasmacites). In an adult, 10 7 clones of in lymphocytes that synthesize 10 7 species of γ-globulins. Glycoprotein γ-globulines consist of 2 heavy (440 AK) and 2 lungs (220 AC) of polypeptide circuits of various configurations that are connected by disulfide bridges. Heterogeneous antibodies, separate components of polypeptides are encoded by different genes, with different mutation ability.

All γ-globulins are divided into 5 classes.G, A, M, D, E . In each class, several subclasses are distinguished.

Disproteinemia Due to the γ-globuline fraction may occur at 1). Immunodeficiency condition; 3). Infectious processes. 2). Neftyal syndrome.

Spicy Phase Phase proteins

The concept of "spicy phase proteins" combines up to 30 plasma proteins of blood, participating in the reaction of the inflammatory response of the body for damage. The proteins of the acute phase are synthesized in the liver, their concentration varies significantly and depends on the stage, the flow of the disease and the massiveness of the damage.

The synthesis of proteins of the acute phase of inflammation in the liver stimulate: 1). IL-6, 2); IL-1 and similar to it (IL-1 A, IL-1R, the factors of necrosis of TNF-OS tumors and FNO-P); 3). Glucocorticoids; four). Growth factors (insulin, hepatocyte growth factors, fibroblasts, platelets).

5 groups of proteins of acute phase are isolated

1. The "main" proteins of the acute phase in humans are C-reactive protein (SRV) and amyloid and protein Serum. The level of these proteins increases during damage very quickly (in the first 6-8 hours) and significantly (20-100 times, in some cases - 1000 times).

2. Proteins whose concentration can increase 2-5 times within 24 hours. it sour α1-glycoprotein, α1-antitripsein, fibrinogen, Gaptoglobin .

3. Proteins whose concentration during inflammation or does not change or increases slightly (20-60% of the initial). it ceruloplasmin, Complement C3 component .

4. Proteins involved in the acute phase of inflammation, the concentration of which, as a rule, remains within the normal range. it α 1 -machroglobulin, hemoplexin, amyloid r protein serum, immunoglobulins .

5. Proteins, the concentration of which when inflammation can decrease by 30-60%. it albumin, Transferin, HDLP, Prehale . A decrease in the concentration of individual proteins in the acute phase of inflammation may be due to a decrease in synthesis, an increase in consumption, or by changing their distribution in the body.

A number of proteins of the acute phase has antiprotein activity. This is α 1 -anttripsin, antihymotripsis, α 2 -machroglobulin. Their important function consists in inhibiting the activity of elastaz-like and chymotrypod-like proteinases coming from granulocytes into inflammatory exudates and causing secondary damage to tissues. Reducing the levels of proteinase inhibitors during septic shock or acute pancreatitis is a bad prognostic feature.

Paraproteinemia - The appearance in the blood plasma of uncharacteristic proteins.

For example, α-fetoglobulin, carcinoembrium antigen can appear in the α-globulin fraction.

α-fetoglobulin - One of the fetal antigens, which circulate in the blood of about 70% of patients with primary hepatoma. This antigen is also detected in patients with stomach cancer, prostate gland and primitive egg tumors. The study of blood for the presence of α-fetoprotein is useful for diagnosing hepatom.

Carcinoembrium antigen (CEA) - Glycoprotein, tumor antigen, characteristic of the intestinal, liver and pancreas of the fetus. The antigen appears in the adenocarcinomas of the gastrointestinal and pancreas organs, in sarcoma and lymphomas, is also found in a number of non-tuch states: with alcoholic cirrhosis of the liver, pancreatite, cholecystitis, diverticulitis and ulcerative colitis.

Plasma enzymes of blood

Enzymes in the blood plasma can be divided into 3 main groups:

1. Secretory . They are synthesized in the liver, intestinal endothelium, vessels enter the blood, where they perform their functions. For example, the enzymes of the coagulation and antoslate blood system (thrombin, plasmin), enzymes of lipoprotein exchange (LHAT, LPL).

2. Fabric . Enzymes of organs of organs and tissues. They fall into the blood with an increase in the permeability of cell walls or during the death of tissue cells. Normally, their blood content is very low. Some tissue enzymes are diagnostic value, because on them you can define an affected organ or tissue, therefore they are also called them indicative . For example, LDH enzymes with 5 isoforms, creatinecinase with 3 isoforms, AST, Alt, sour and alkaline phosphatase, etc.

3. Excretory . Enzymes synthesized by the glands of the gastrointestinal tract (liver, pancreas, salivary glands) in the lumen of the LCD tract and participating in digestion. In the blood, these enzymes appear during damage to the corresponding glands. For example, with pancreatitis in the blood, lipase, amylase, trypsin are found, with inflammation of the salivary glands - amylase, with cholestasy - alkaline phosphatase (from the liver).


Fraction

Proteins

End

g / l

Function

albumin

Transstitutein

0,25

Albumen

Maintaining osmotic pressure, veins of fatty acids, bilirubin, grained acids, steroid hormones, drugs, inorganic ions, reserve amino acids

α 1 -Globulins

α 1 -Antrippsin

Proteinase inhibitor

Sour α 1 - Glycoprotein

Transport Progesterone

Prothrombin

Blood Cut Factor II

Transcortin

0,03

Cortisol transport, Corticosterone, progesterone

Tyroxins binding globulin

0,02

Trojoxin and triiodothyronine transport

α 2 -Globulins

Ceruloplasmin

0,35

Transportation of copper ions, oxidoreductase

Antithombin III

Inhibitor of plasma proteases

Gaptoglobin

Binding hemoglobin

α 2 -Makroglobulin

Plasma proteases inhibitor, zinc transport

Retinol binding protein

0,04

Retinol transport

Vitamin D binding protein

Transportation of calciferol

β-globulins

LDL.

Transport cholesterol.

Transfirin

Vehicle ions transport

Fibrinogen

Factor I Cutting Blood

TransCobalammin

25*10 -9

Vitamin C 12

Globulin binding protein

20*10 -6

Testosterone and estradiol transport

C-reactive protein

< 0,01

Activation of complement

γ-globulins

Late antibodies

Antibodies protecting mucous membranes

Early antibodies

0,03

B-lymphocyte receptors

< 0,01

Value plasma proteins of blooddifficult:

  1. Proteins determine the occurrence of oncotic pressure (see below), the magnitude of which is important for regulating the water exchange between blood and tissues.
  2. Proteins, possessing buffer properties, support acid-alkaline blood equilibrium.
  3. Proteins provide blood plasma a certain viscosity, which is important in maintaining blood pressure.
  4. Plasma proteins contribute to blood stabilization, creating conditions that prevent erythrocyte settlement.
  5. Plasma proteins play an important role in blood clotting.
  6. Plasma proteins are important immunity factors, i.e. immunity to infectious diseases.

The blood plasma contains several dozen different proteins that make up three main groups: albumin, globulins and fibrinogen. For the separation of plasma proteins since 1937, the electrophoresis method is used, based on the fact that different proteins have unequal mobility in the electric field. With the help of electrophoresis, globulins are separated into several fractions: α1-, α2-, β and γ - globulins.

Electrophoretic diagram plasma proteins of blood given on fig. one. Gamma-globulins are essential in protecting the body from viruses, bacteria and their toxins.

This is due to the fact that the so-called antibodies are mainly γ-globulin. The introduction of their patients increases the body's resistance in relation to infections. Recently, a protein complex has been found in the blood plasma, which plays a similar role, - Propernin.

The ratio between the number of different protein fractions in some diseases changes and therefore the study of the protein fraction has a diagnostic value.

The main place of formation of plasma proteins is a liver. It synthesizes albumin and fibrinogen. Globulines are synthesized not only in the liver, but also in the bone marrow, spleen, lymph nodes, i.e., in organs relating to the reticulous endothelial system of the body. In the entire blood plasma contains approximately 200-300 g of proteins. The exchange of them occurs quickly due to continuous synthesis and decay.

Fig.1. The separation of the human blood plasma proteins obtained during electrophoresis.

Osmotic blood plasma protein pressure

It is created not only by crystaloids dissolved in blood plasma, but also by colloids - plasma proteins. Osmotic pressure due to them is called oncotic.

Although the absolute amount of blood plasma proteins is 7-8% and almost 10 times exceeds the amount of dissolved salts created by them oncotic pressure is only about 1/200 of the plasma osmotic pressure (equal to 7.6-8.1 atm.), T . e. 0.03-0.04 atm. (25-30 mm Hg. Art.). This is due to the fact that protein molecules have very large sizes and the number of them in plasma many times less than the number of crystalloid molecules.

Despite its small amount, oncotic pressure plays an extremely important role in the exchange of water between blood and tissues. Oncotic pressure affects the physiological processes, which are based on the filtration phenomena (the formation of the interstitial fluid, lymph, urine, water absorption in the intestine). Large plasma protein molecules, as a rule, do not pass through the endothelial wall of the capillaries. Staying inside the bloodstream, they retain some amount of water in the blood (in accordance with the magnitude of their osmotic pressure). By this, they contribute to the preservation of the relative constancy of water content in the blood and tissues.

The ability of blood proteins to hold water in vascular bed can be proved by the following experience. If the dog has repeated bloodsucms and, with the help of centrifugation, separate the plasma of the blood from the red blood cells, and the last to be brought back into the blood in the saline solution, then in such a way you can strongly reduce the number of proteins in the blood. At the same time, there are significant edema in the animal. In an experiment with isolated organs with prolonged passing through them, Ringer's solution or Ringer - Locke comes with tissue edema. If we replace the physiological solution of blood serum, then the edema that started can be destroyed. This explains the need to bring colloidal substances into the blood-blowing solutions. In this case, the oncotic pressure and viscosity of such solutions are chosen so that they are equal to viscosity and oncotic blood pressure.

Biochemistry of blood

Question 61.

The blood plasma contains 7% of all organism proteins at a concentration of 60 - 80 g / l. Plasma proteins of blood perform many functions. One of them is to maintain osmotic pressure, since proteins bind water and hold it in the bloodstream.

  • Plasma proteins form an essential buffer blood system and maintain blood pH within 7.37 - 7.43.
  • Albumin, transstaretin, transcortin, transferin and some other proteins (Table 14-2) pushing the transport function.
  • Plasma proteins determine blood viscosity and, therefore, play an important role in hemodynamics of the circulatory system.
  • Blood plasma proteins are a reserve amino acids for the body.
  • Immunoglobulins, proteins of blood flowing system, α 1 -anttripsin and complement proteins are protective function.

The method of electrophoresis on acetylcellulose or gel of agarose plasma proteins can be divided into albumin (55-65%), α 1 -Globulins (2-4%), α 2 -Globulins (6-12%), β-globulines (8-12 %) and γ-globulines (12-22%) (Fig. 14-19).

The use of other media for electrophoretic separation of proteins allows you to detect a greater number of fractions. For example, with electrophoresis in polyacrylamide or starch gels in the blood plasma, 16-17 protein fractions are distinguished. The immunoelectrophoresis method combining the electrophoretic and immunological analysis methods allows to divide blood plasma proteins by more than 30 fractions. Most serum proteins are synthesized in the liver, but some are formed in other tissues. For example, γ-globulins are synthesized in lymphocytes (see section 4), peptide hormones mainly secrete cells of endocrine glasses, and the peptide hormone erythropoietin - kidney cells. For many plasma proteins, such as albumin, α 1 -anttripsin, haptoglobin, trans-ferrine, cerululosmin, α 2 -machroglobulin and immunoglobulins are characterized by polymorphism (see section 4). Almost all plasma proteins, with the exception of albumin, are glycoproteins. Oligosaccharides are joined by proteins, forming glycosida ties with a hydroxyl group of serine or threonine, or interacting with the carboxyl group asparagin. The end balance of oligosaccharides is in most cases a N-acetylneiramic acid connected to galactose. The endothelium enzyme neuraminidase vessels hydrolyzys the connection between them, and the galactose becomes available for specific hepatocyte receptors. By euddcitosis, "aged" proteins come into liver cells, where they are destroyed. T 1/2 Plasma proteins of blood ranges from several hours to several weeks. With a number of diseases, a change in the ratio of the distribution of protein fractions during electrophoresis compared with the norm (Fig. 14-20). Such changes are called disproteinemia, but their interpretation often has relative diagnostic value. For example, a decrease in albumines, α 1 - and γ-globulins characteristic of nephrotic syndrome and an increase in α 2 - and β-globulins is also observed in some other diseases accompanied by loss of proteins. With a decrease in humoral immunity, the decrease in the γ-globulin fraction indicates a decrease in the content of the main component of immunoglobulins - IgG, but does not reflect the dynamics of IGA and IGM changes. The content of some proteins in the blood plasma can sharply increase in acute inflammatory processes and some other pathological conditions (injuries, burns, myocardial infarction). Such proteins are called proteins of the acute phase, as they participate in the development of the inflammatory response of the body. The main inductor of the synthesis of most proteins of the acute phase in hepatocytes is the interleukin-1 polypeptide, exempt from mononuclear phagocytes. The proteins of the acute phase include a C-jet protein, called so, because it interacts with the C-polysacharium-house of pneumococci, α 1 -anttripsin, haptoglobin, acidic glycoprotein, fibrinogen. It is known that the C-jet protein can stimulate


Fig. 14-19. Electrophoregram (a) and densitogram (b) proteins of blood serum.

Fig. 14-20. Proteinograms of serum proteins. a - normally; b - with nephrotic syndrome; in - with hypogammaglobulinemia; g - with cirrhosis of the liver; d - with a lack of α 1 -anttripsin; E - with diffuse hypergammaglobulinemia.

complement system, and its blood concentration, for example, with exacerbation of rheumatoid arthritis may increase by 30 times compared with the norm. Blood plasma protein A, -Antrippsin can inactivate some proteases released in the acute phase of inflammation.

Albumen.The concentration of albumin in the blood is 40-50 g / l. About 12 g of albumin, T 1/2 of this protein is synthesized in the liver, about 20 days. Albumin consists of 585 amino acid residues, has 17 disulfide bonds and has a molecular weight of 69 kD. Albumin molecule contains many dicarboxylic amino acids, therefore, it can keep the Ca 2+ cations in the blood, Cu 2+, Zn 2+. About 40% of albumin is contained in the blood and the remaining 60% in the intercellular fluid, however its plasma concentration is higher than in the intercellular fluid, since the volume of the latter exceeds the volume of the plasma 4 times.

Due to the relatively small molecular weight and high concentration, albumin provides up to 80% of the osmotic pressure of the plasma. With hypoalbuminemia, the osmotic pressure plasma pressure is reduced. This leads to a violation of equilibrium in the distribution of extracellular fluid between the vascular channel and the intercellular space. Clinically, this is manifested as an edema. The relative decrease in the volume of blood plasma is accompanied by a decrease in the renal blood flow, which causes the stimulation of the Rennanangiotenzinalroneon system, which ensures the reduction of blood volume (see section 11). However, with a lack of albumin, which must hold Na +, other cations and water, water goes into the intercellular space, enhancing the edema.

Hypoalbuminemia can also be observed as a result of a decrease in the synthesis of albumin in the diseases of the liver (cirrhosis), with an increase in capillaries permeability, with the loss of protein due to extensive burns or catabolic states (heavy sepsis, malignant neoplasms), with nephrotic syndrome, accompanied by albuminuria and starvation. Disturbance of blood circulation, characterized by a slowdown in blood flow, lead to an increase in albumin's admission to the intercellular space and the appearance of edema. A rapid increase in permeability of capillaries is accompanied by a sharp decrease in blood volume, which leads to a drop of blood pressure and clinically manifested as shock.

Albumin is the most important transport protein. It transports free fatty acids (see section 8), non-conjugated bilirubin (see section 13), Ca 2+, Cu 2+, tryptophan, thyroxine and triiodothyronine (see section 11). Many medicines (aspirin, dickyurol, sulfonamides) are associated with albumin. This fact must be taken into account in the treatment of diseases accompanied by hypoalbuminemia, since in these cases the concentration of free medication in the blood increases. In addition, it should be remembered that some drugs can compete for binding centers in albumin molecule with bilirubin and among themselves.

Transstitutein(Prehaletbin) is called the tick-syncing prehalation. This is a protein of the acute phase. Transdutentine belongs to the fraction of albumin, it has a tetramer molecule. It is able to attach a retinol binding protein in one binding center, and in the other - up to two thyroxine and triiodothyronine molecules.

Table 14-2. Content and functions of some blood plasma proteins

Power supply (on 3 liters of plasma there are 200 g of protein) is a sufficient supply of nutrients.

Transportation - due to the presence of hydrophilic and hydrophobic areas, proteins are capable of binding to molecules and leafy-like substances and carrying out their transfer to blood. Plasma proteins bind 2/3 plasma calcium.

The oncotic pressure plasma pressure is largely (80%) depends on albumin (less molecular weight, but more plasma than globulins). Reducing the concentration of albumin leads to a delay of H 2 o in the intercellular space (interstitial swelling).

Buffer function - maintains the constancy of blood pH by binding H + or it -, thanks to amphoteric properties.

Prevention of blood loss is due to the presence of fibrinogen blood in plasma. The high viscosity of the fibrinogen solutions is due to the property of its molecules to form clots in the form of "thread beads". The chain of the hemostasis reactions in which plasma proteins are involved ends with the conversion of fibrinogen dissolved in the plasma to a network of fibrin molecules forming a clot (Trombus). Fibrin molecule has an extended shape (ratio of length / width - 17: 1).

Properties and functions of individual protein fractions.

Plasma albumin by 80% determines the colloid-osmotic (oncotic) plasma pressure. It accounts for 60% of the total plasma protein (35-45 g / l).

Albumin is a low molecular weight compound and therefore well suited to perform the function of the carriers of many blood translated substances. Albumin binds: Billirubin, urobilin, fatty acids, bile acid salts, penicillin, sulfamin, mercury.

With inflammatory processes and lesions of the liver and kidney, the amount of albumin decreases.

Globulins.

a 1 - Globulins, otherwise they are called glycoproteins. 2/3 of the total plasma glucose is present in the bound form in the composition of glycoproteins. The subfractions of glycoproteins includes a group of carbohydrate proteins - proteoglycans (mucoproteins).

a 2 - Globulins are proteoglanic or otherwise copper-containing cerulululzmin protein, which connects 90% of all copper contained in the plasma.



b-globulin is protein lipid and polysaccharide carriers. They hold in the solution insoluble in water fats and lipids and thereby ensure their transfer of blood.

g - Globulins. This is an inhomogeneous group of proteins that perform protective and neutralizing functions, otherwise called immunoglobulin. The dimensions and composition G - globulin varies significantly. With all diseases, especially inflammatory, the content of G - globulins in the plasma rises. G-Globulins include blood agglutinins: anti-a and anti-c.

Erythrocytes

The most numerous uniform blood elements are red blood tales (red blood cells). In men - 4 - 5 million in 1 mk; In women, as a rule, does not exceed 4.5 million in 1 μl. During pregnancy, the number of erythrocytes can decrease to 3.5 and even 3 million in 1 μl.

Normally, the number of erythrocytes is subject to insignificant oscillations.

With different diseases, the number of erythrocytes may decrease ("erythroaction"). This often accompanies anemia or anemia.

An increase in the number of erythrocytes is indicated as "erythrocytosis".

Human erythrocytes are nuclear-free, flat cells having the shape of two-screwed discs. Their thickness in the region of the edges - 2MKM.

The surface of the disk is 1.7 times larger than the body surface of the same volume, but spherical form. Consequently, this form provides transport of a large number of different substances. This form allows erythrocytes to be fixed in the fibrin network in the formation of a thrombus. But the main advantage is that this form ensures the passage of red blood cell through the capillaries. In this case, the erythrocyte twisted in the middle narrow part, the contents from the wider end flows to the center, making the erythrocyte in a narrow capillary.

The cytoskeleton in the form of tubes passing through the cell and microfilaments in the erythrocyte is absent, which gives it elasticity and deformability (the necessary properties for passing through the capillaries).

Jones Curve - This is the distribution of erythrocytes in diameter. The distribution of erythrocyte diameters is normal correspond to the normal distribution curve.

Normation - the average size of the erythrocyte diameter in an adult is 7.5 microns. (7.5 - 8.3 μm).

Macrocytes - erythrocyte diameter from 8 to 12mkm. Macrocytosis is observed during the shifts of the curve to the right.

Microcytes - the diameter of erythrocytes less than 6 microns - the shift of the curve left. Dwarf erythrocytes with shortened lifespan are found.

The field shape of the price-johns curve indicates an increase in the number of both microcytes and macrocytes. This phenomenon is called anisocytosis.

Erythrocytes have reversible deformation, that is, they possess plasticity.

As aging, the plasticity of the erythrocytes decreases.

The most famous pathologically modified form of red blood cells is spherocytes (round-form erythrocytes) and sickle erythrocytes (SKA).

Poikilocytosis - The condition at which erythrocytes of different unusual shapes are found.

Erythrocyte functions: transport, protective, regulatory.

Transport function: transport about 2 and CO 2, amino acids, polypeptides, proteins, carbohydrates, enzymes, hormones, fats, cholesterol, bava, trace elements, etc ..

Protective function: Play a specific role in specific and non-specific immunite, take part in vascular-platelet hemostasis, blood coagulation and fibrinolysis.

Regulatory function: Thanks to hemoglobin, blood pH is regulated, the ion composition of the plasma and water exchange.

Penetrated into the arterial end of the capillary, the erythrocyte gives water and dissolved in it about 2 and decreases in the amount, and turning into the venous end of the capillary, takes water, CO 2 and the exchange products coming from tissues and increases in volume.

Help maintain the relative constancy of blood plasma. For example, if the plasma increases proteins concentration, the red blood cells are actively adsorbed. If the content of plasma proteins decreases, the erythrocytes give them to the plasma.

Erythrocytes are regulators of erythropoese, because They contain erythropoietic factors that, in the destruction of the erythrocytes, enter the bone marrow and contribute to the formation of erythrocytes.

Erythropoes is the process of formation of red blood cells.

Erythrocytes are formed in hematopoietic fabrics:

In the yolk bag at the embryo

In the liver and spleen from the fetus

In the red bone marrow of the flat bones in an adult.

Common predecessors of all blood cells are pluripotent (polypotent) stem cells, which are contained in all hematopoietic organs.

At the next stage of erythropoese, combined precursors are formed, from which only one type of blood cells can already develop: red blood cells, monocytes, granulocytes, platelets or lymphocytes.

Table cage → Basophilic passriblast → Erythroblast (Macoblast) → Normoblast → Reticulocytes II, III, IV → Erythrocytes.

Non-surgeful young erythrocytes exit bone marrow in the form of so-called reticulocytes. In contrast to red blood cells, reticulocytes retain elements of cellular structures. The number of reticulocytes is an important information on the state of erythropoese. Normally, the number of reticulocytes is 0.5 - 2% of the total number of blood erythrocytes. When erythropoede accelerates, the number of reticulocytes increases, and when the erythropoese is slowed down, it decreases. With enhanced destruction of erythrocytes, the number of reticulocytes may exceed 50%. The transformation of the reticulocyte in a young erythrocyte (normocyte) is carried out in 35-45 hours.

Ripened erythrocytes are circulated in the blood for 80-120 days, after which they are phased mainly by the cells of the ReticuloNothelial bone marrow system, macrophages ("erythrofagocytosis"). The products formed about this and primarily iron are used to build new erythrocytes. Castle introduced the concept of "erythron" to designate the entire mass of erythrocytes in circulating blood, in blood depot and bone marrow.

Any body fabric is also capable of destroying red blood tales (the disappearance of "bruises").

Every 24 hours is updated approximately 0.8% of the total number of erythrocytes (25 · 10 12 pcs). For 1 min, 60 · 10 6 erythrocytes are formed.

The speed of erythropois is increasing several times

With blood loss

With a decrease in the partial pressure of 2

Under the action of substances of accelerating erythropoese - erythropoethines.

Place of synthesis of erythropoethines - kidneys, liver, snarling, bone marrow. Erythropoetins stimulates differentiation and accelerates the reproduction of erythrocyte predecessors in the bone marrow.

The effect of erythropoietina is enhanced: androgens, thyroxin, growth hormones.

Androgens are enhanced by erythropoes, and estrogens brake erythropoes.

Osmotic properties of red blood cells.

When placing erythrocytes in the hypotonic solution, hemolysis is developing - this is the rupture of the erythrocyte shell and the hemoglobin output in the plasma, so that the blood acquires a varnish color. The minimum hemolysis border for healthy people corresponds to a solution containing 0.42 - 0.48% NaCl. The maximum border of resistance is 0.28 - 0.34% NaCl.

The causes of hemolysis can also be chemical agents (chloroform, ether, etc.), the poisons of some snakes (biological hemolysis), the effects of low and high temperatures (thermal hemolysis), incompatibility of blood transfusional (immune hemolysis), mechanical effects.

Erythrocyte sedimentation rate (SE).

Blood provides a suspension or suspension of erythrocytes. The suspension of plasma erythrocytes is maintained by the hydrophilic nature of their surface, as well as a negative charge, so that they are repelled from each other. With a decrease, negative erythrocytes face each other by forming the so-called "coin columns".

Farreus - by placing blood into the test tube, after adding the Na citrate, (which prevents blood coagulation) found that the blood is divided into two layers. The bottom layer is uniform elements.

The main reasons affecting the erythrocyte sedimentation rate:

The magnitude of the negative charge on the surface of the erythrocytes

The magnitude of the positive charge of plasma proteins and their properties

Infectious, inflammatory and oncological diseases.

The value of the SE is more depends on the properties of the plasma than from the properties of the erythrocytes. Example if normal erythrocytes of men are placed in the plasma of the blood of a pregnant woman, then the red blood cells will settle with the same speed as women during pregnancy.

Soe - in newborns - 1-2 mm / h; In men - 6-12 mm / h; In women - 8-15 mm / h; The elderly - 15-20 mm / h.

ESP increases with increasing fibrinogen concentration, for example during pregnancy; with inflammatory, infectious and oncological diseases; and also with a decrease in the number of erythrocytes. The decrease in ESP in children over 1 years old is considered an unfavorable sign.

Hemoglobin and its connections.

The main functions of the erythrocytes are caused by the presence of hemoglobin in their composition. Its molecular weight is 68800. Hemoglobin consists of a protein part (globin) and iron-containing parts (gem) 1: 4 (per molecule of GLUSIN there are 4 heme molecules).

The gem consists of a porphyrin molecule, in the center of which the FE 2+ ion is located capable of attaching 2.

The structure of the protein part of hemoglobin non-etinakova, i.e. The protein part of the hemoglobin can be divided into a number of fractions: and the fraction is 95-98% for an adult; And 2 fraction - 2-3%; F fraction - 1-2%.

Fraction F is fetal hemoglobin, which is contained by the fetus. Fetal hemoglobin has a greater affinity for 2 than hemoglobin A. By the time of the birth of a child on his share accounts for 70-90%. This allows the fetus tissues without testing hypoxia at a relatively low voltage of 2.

Hemoglobin has the ability to form connections from O 2, CO 2 and CO:

hemoglobin C O 2 (gives light red blood) - called oxymemoglobin (HHBO 2);

hemoglobin who gave 2 is called restored or reduced (HHB);

hemoglobin with CO 2 is called carbohemoglobin (HHBCO 2) (dark blood) 10-20% of total blood transported by 2;

hemoglobin with CO forms a durable carboxygemoglobin bond (HHBCO), the affinity of hemoglobin to with higher than to 2.

The rate of decay of carboxygemoglobin increases when inhalation is pure 2.

Strong oxidizers (ferrocyanide, bertolet salt, hydrogen peroxide) change Fe 2+ charge to Fe 3+ - oxidized hemoglobin methemoglobin occurs, a solid connection to 2; Transportation of O 2 is violated, which leads to the most severe consequences for humans and fatal outcome.

In the event of the destruction of erythrocytes, bilirubin is formed from the freed hemoglobin, which is one of the components of bile.

Color indicator (Farb Index Fi).

The relative value that characterizes the saturation of 1 erythrocyte hemoglobin. For 100% hemoglobin takes a value equal to 166.7 g / l, and for 100% erythrocytes - 5 * 10 12. If a person has content and hemoglobin and erythrocytes 100%, then the color indicator is 1.

It is calculated by the formula: CPU \u003d HB (g / l) * 3 / (the three first numbers from the number of erythrocytes).

Normally from 0.85 to 1.15 (normochromic red blood cells). If less than 0.85 - hypochromic erythrocytes. If more than 1.15 are hyperchromic. In this case, the volume of erythrocyte increases, which allows it to contain a large concentration of hemoglobin. A false impression is created that the erythrocytes are oversaturated with hemoglobin.

Gyuo- and hyperchromy are found under anemia.

Anemia.

Anemia (Breakfold) is a decrease in the ability to transfer oxygen associated either with a decrease in the number of erythrocytes, or with a decrease in the content in hemoglobin erythrocytes, or both.

Ironingful anemia occurs with a lack of iron in food (in children), with impairment of iron absorption in the digestive tract, with chronic blood loss (ulcerative disease, tumors, colitis, melted invasions, etc.). In the blood, small erythrocytes with a reduced hemoglobin content are formed.

Megablastic anemia - the presence of increased red blood cells (megalocytes) in the blood and bone marrow and the immature predecessors of megalocytes (megablasts). It occurs with the lack of substances contributing to the ripening of erythrocytes (vitamin B 12), i.e. With slow-down ripening of red blood cells.

Hemolytic anemia is associated with the increased fragility of red blood cells, which leads to increasing hemolysis. The reason is congenital forms of spherocytosis, sickle cell anemia and thalassemia. The same category includes anemia arising in malaria, with rhesus incompatibility.

Aplastic anemia and barbecue is the oppression of bone marrowing. Erythropoes is suppressed. The reason is hereditary shape and / or bone marrow damage by ionizing radiation.

6.3. Leukocytes

White blood tales (leukocytes) are the formation of various shapes and values. They are divided into two large groups:

granular (granulocytes): neutrophils, eosinophils, basophiles

invalid (agranulocytes): lymphocytes, monocytes.

Granulocytes received the name from their ability to be painted with paints: eosinophils are painted with eosin (acid paint), basophiles - hematoxylin (alkaline paint), and neutrophils - and the other.

Normally, the number of leukocytes in adults fluctuates from 4.5 to 8.5 thousand in 1 mm 3. Increased leukocyte is called - leukocytosis. Reduced - leukopenia.

Leukopenia is found only in pathology. Especially severe in the case of bone marrow lesions (sharp leukemia, radiation disease). At the same time, the number of leukocytes is not only reduced, but also change their functional activity. There are disorders in specific and non-specific protection, associated diseases (often infectious nature).

Leukocytosis can be physiological and pathological. Physiological leukocytosis: food; miogenous; emotional; during pregnancy.

Food leukocytosis. It occurs after meals (an increase of 1-3 thousand in 1 μl), rarely goes beyond the boundaries of the physiological norm. A large number of leukocytes accumulates in a subtle intestinal basis. Here they carry out a protective function, prevent foreign agents in the blood and lymph.

It is redistributive. Provided by the receipt of leukocytes in blood flow from the bloodstream.

Moiogenic leukocytosis. It is observed after performing heavy muscle work. The number of leukocytes can increase 3-5 times. Leukocytes accumulate in the muscles. Wears both redistributive and true character, because In this leukocytosis, bone marrowing is increased.

Emotional leukocytosis (as in pain irritation) is awarded. Rarely reaches high indicators.

Leukocytosis during pregnancy. Accumulate in the submucosity of the uterus. This leukocytosis is mainly local. This leukocytosis prevents infections from entering and stimulates the contractile function of the uterus.

Leukocyte formula (leukogram).

In the blood can occur mature and young forms of leukocytes. Normally, they are easier to detect them from the largest group, i.e. In neutrophils. Young neutrophils (myelocites) have a rather large bean-like core. Shard-core - the kernel, not divided into separate segments. Mature, or segmented, have a kernel, divided into 2-3 segments. The more segments, the older neutrophil.

An increase in the number of young and pulp neutrophils indicates blood rejuvenation is a shift of the leukocyte formula to the left (leukemia, protein, infection, inflammation). A decrease in the number of these cells indicates blood aging is the leukocyte formula shift to the right.

Neutrophils.

Ripen in the bone marrow, delayed in it for 3-5 days, constituting the bone marrow reserve of granulocytes. The vascular channel falls due to the amoeboid movement and the release of proteolytic enzymes that can dissolve bone marrow proteins and capillaries.

In the circulating blood neutrophils live from 8 hours to 2 days. Conventionally divided by: 1) freely circulating; and 2) occupying the edible position in the vessels. There are dynamic equilibrium between these groups and constant exchange. So In the vascular bed, about 2 times more neutrophils than is determined in the flowing blood.

It is assumed that the destruction of neutrophils occurs outside the vascular bed. All leukocytes go into fabrics, where they die. Possess phagocytic function. Absorb bacteria and tissue destruction products.

In 1968, a cytotoxic effect was opened, or a killing. In the presence of IgG and in the presence of complement, it is suitable for a target cell, but not phagocyt, and they are damaged at a distance, due to the isolation of the active forms of oxygen - hydrogen peroxide, hypochloric acid, etc.

Products that enhance the mitotic activity of cells, accelerating the processes of reparation, stimulating hemopoies and dissolving the fibrin bunch.

In clinical practice, it is necessary to investigate not only the quantity, but also the functional activity of neutrophils. The hypofunction of neutrophils is an immunodeficiency option. It is manifested in reducing the migration ability and bactericidal activity of neutrophils.

Basophiles.

There are few basophils (40-60 in 1 μl), but in various tissues, including in the vascular wall, contain "tissue basophiles" or fat cells.

Absorption, synthesis, accumulation and allocation of Bav.

Histamine - enhances tissue permeability, expands blood vessels, enhances the hemochaguance, in high concentrations causes inflammation.

Heparin - antagonist of histamine. Anticoagulant (prevents blood coagulation). Inhibits fibrinolysis (fibrin destruction), many lysosomal enzymes, histamine (destroying histamine).

Hyaluronic acid (affects the permeability of the vascular wall).

Factor activation factor.

Thromboxanes (contribute to platelet aggregation).

Arachidonic acid derivatives are an important role in allergic reactions (bronchial asthma, urticaria, dosage disease).

The number of basophils increases with leukemia, stressful situations and slightly when inflammation.

In connection with the release of various forms of basophils and the identification of various BAV, there are synonyms - heparinocyte, histaminocyte, labrocyte, etc. exist.

Bazophil antagonists are eosinophils and macrophages.

Eosinophils.

The duration of the stay of eosinophils in the bloodstream does not exceed a few hours, after which they penetrate the fabric, where they are destroyed.

In the tissues, eosinophils accumulate in those organs where histamine is contained in the mucous membrane and the stomach, small intestine, in the lungs. Eosinophils capture and destroy histamine with the hystamine enzyme. Capable also to inactivate heparin, phagocytic granules allocated by basophilies. These properties are associated with the participation of eosinophils in reducing the reaction of the hypersensitivity of the immediate type.

Phagocytic activity is expressed. Cockki is especially intensely phased.

The role of eosinophils in the fight against helminths, their eggs and larvae (anti-chain immunity) is extremely great. Upon contact of the activated eosinophila with larvae, it is degranulation, followed by the release of a large amount of protein and enzymes (for example, peroxidase) to the surface of the larva, which leads to the destruction of the latter.

Eosinophils are able to bind antigens, preventing them from entering the vascular channel.

Eosinophilah contains cationic proteins that activate the components of the Kallemirinein-kinin system and affect blood coagulation.

With severe infections, the number of eosinophils is reduced. Sometimes they are not detected at all (aoxinople).

Monocytes:

Circulated in the blood to 70 hours, then migrate into the tissue, forming an extensive family of tissue macrophages.

They are extremely active phagocytes, provide cytotoxic effects. The apparatus of lysos is developed containing important enzymes.

The outer plasma membrane contains numerous receptors, including those allowing "learning" immunoglobulins, fragment of the complement, lymphocytes, mediators. Due to this, macrophages do a role not only in cellular nonspecific immunite, but also participate in the regulation of specific immunity. They recognize the antigen, translate it into the immunogenic shape, form biologically active compounds - monokines acting on lymphocytes.

Lymphocytes.

Like other leukocytes, the lymphocytes are formed in the bone marrow, then enter the vascular bed. Part of the lymphocytes receives a "specialization" in the fork iron where they turn into T-lymphocytes (thymus-dependent).

Another population is in lymphocytes (Bursa - in birds). In humans and mammals, their formation occurs in the bone marrow, or in the system of lymphoid-epithelial formations, located in the course of the small intestine (lymphoid or peer plaque).

T-lymphocytes:

T-killers (killers) - carry out lysis (destruction) target cells.

T-helpers (helpers) - enhance cellular immunity.

T-T - helpers - enhance cellular immunity.

T-B - Helpers - enhance humoral immunity.

T-amplifier - reinforce the functional activity of lymphocytes.

T-suppressors - prevent the immune response.

T-T-suppressors - suppress cellular immunity.

T-in-suppressors - suppress humoral immunity.

T - counter-obligressors - prevent the action of T-suppressors and thereby enhance the immune response.

T - cells of immune memory that store information about previously active antigens and regulating the secondary immune response, which develops in a shorter time.

TD lymphocytes (differentiating). The function of stem-formational cells, the ratio of the erythrocyte, platelet, leukocyte sprouts of the bone marrow is adjusted.

In lymphocytes.

Most in lymphocytes in response to the action of antigens and cytokines are transferred to plasma cells, produce antibodies (antibody products).

In addition, among V-lymphocytes distinguish:

B-killers (the same function as T-killers).

B-helpers - reinforce the effect of TD lymphocytes and T-suppressors.

Populars - inhibit antibodies proliferation.

There are neither T-, nor in lymphocytes - 0 lymphocytes (predecessors of T- and B-lymphocytes).

Some researchers for 0 lymphocytes include NK lymphocytes (natural killers).

There are cells that carry markers and T- and B-lymphocytes (double cells) are capable of replacing both those and others.

Cytotoxic effects:

Secrets proteins capable of hardening holes in alien cell membranes. Contain proteolytic enzymes (cytolysis), which penetrate the alien cell through the resulting pores and destroy it.

IMMUNITY

Immunity - a way to protect the organism from living bodies and substances carrying signs of alien genetic information.

Immunological regulation on the one hand is an integral part of humoral, since most processes are carried out with the direct participation of humoral intermediaries. However, the immune regulation is essentially aims, and thus reminds nervous regulation. Lymphocytes and monocytes, as well as other cells participating in an immune response, give a humoral mediator directly target organ. Hence the immunological regulation is called cell-humoral.

The immune system is represented by all types of leukocytes, as well as organs in which leukocyte development occurs: bone marrow, thymus, spleen, lymph nodes.

Split nonspecific and specific immunities:

1. Nonspecific - directed against any alien substance (antigen). Manifests in the form of humoral - products of bactericidal substances; and cell - phagocytosis, cytotoxic effect (1968 ...)

Phagocytosis is inherent in: neutrophilas, eosinophils, monocytes, macrophages. The cytotoxic effect is also lymphocytes.

2. Specific - directed against a certain alien substance. Also in 2 forms: humoral - products of antibodies in lymphocytes and plasma cells and cellular - with the participation of T-lymphocytes.

In the immune response, the mechanisms of both humoral and cellular immunity are usually operated, but in different degrees (for measles, a humoral response is dominated, with cellular allergies).

In the blood plasma of human contains approximately 200-300 g of protein. Plasma proteins are divided into two main groups: albumin and globulins. The globulin fraction includes fibrinogen.

Albumin 60% of plasma proteins are highly concentrated (about 80%), high mobility at relatively small sizes of the molecule; Participate in the transport of nutrients (amino acids), as well as a number of other substances (bilirubin, heavy metals salts, fatty acids, drugs).

Globulins. These include groups of large-molecular weight proteins, which have lower mobility than albumin. Among globulins can be allocated beta globulinsParticipated in the transport of steroid hormones, cholesterol. They hold about 75% of all fats and plasma lipids.

Another group of these proteins - gamma globulinscomprising various antibodies protecting the body from invasion of viruses and bacteria. These include also aggulutinina blood plasma. Fibrinogen It occupies an intermediate position between the above proteins. It has a property to move into an insoluble fibrous shape - fibrin - under the influence of thrombin enzyme. In fibrinogen blood plasma, only 0.3% is contained, but it is its participation that the blood coagulation is determined and its transformation within a few minutes into a dense bunch. The serum of blood is different from plasma in the absence of fibrinogen.

Albumin and fibrinogen are formed in the liver, globulins - in the liver, bone marrow, spleen, lymph nodes. In the human body, 17 g of Albumin and 5 g of Globulin are produced during the day. The half-life of albumin is 10-15 days, Globulin - 5 days.

Plasma proteins together with electrolytes (CA 2+, K +, NA +, etc.) are its functional elements. They are involved in the transport of substances from the blood to the tissues; Transport nutrients, vitamins, trace elements, hormones, enzymes, as well as final metabolic products. Plasma proteins also participate in maintaining permanent osmotic pressure, as they can bind a large number of low molecular weight circulating blood. Proteins created oncotic pressure It plays an important role in regulating water distribution between plasma and intercellular fluid. It is 25-30 mm Hg. Art. Thus, the value of proteins is very large and is as follows:

Proteins are buffer substances, while maintaining the constancy of the blood reaction;



Proteins cause blood viscosity, which is of great importance for maintaining constancy of blood pressure;

Proteins play an important role in aquatic exchange. The exchange of water between blood and tissues, the intensity of urine formation, largely depends on their concentration. Proteins are factors of immunity formation;

Fibrinogen is the main factor in blood coagulation.

With age, the content of proteins in the plasma increases. By 3-4 years, the protein content practically reaches the level of adults (6.83%). In early age, there are wider boundaries of the oscillations of protein content (from 4.3 to 8.3%) compared with adults whose oscillation limits from 7 to 8%. The smallest amount of protein is noted up to 3 years, then the amount of protein increases from 3 to 8 years. In subsequent periods, it increases slightly. In prepubertal and pubertal age, the protein content is more than in childhood and middle ages.

The newborns reduced the content of albumin (56.8%) with relatively high content of gamma globulin. The content of albumin gradually increases: by 6 months it averages 59.25%, and by 3 years - 58.97%, which is close to the norm of an adult.

The level of gamma globulin is high at the moment of birth and in early posts of postnatal life by obtaining them from the mother through the placental barrier. During the first 3 months, their destruction occurs and the drop in the blood level. Then the content of gamma globulins increases slightly, reaching by 3 years of an adult (17.39%).

Blood cells, their characteristics, functions. Age features.Blood cells (or uniform elements) are divided into red blood tales - red blood cells, white blood tales - leukocytes and blood plates - platelets (atl., Fig. 2, p. 143). The total volume of their person is about 44% of the total blood volume.

The classification of blood shaped blood elements can be represented as follows (Fig. 16).



Erythrocytes
Blood cells Ý Leukocytes Ý Granular leukocytes Ý Eosinophila
Ý Basophiles
Ý Neutrophila
Invalid leukocytes Ý Monocytes.
Ý lymphocytes Ý B-lymphocytes
Ý Plasmocytes
Ý T-lymphocytes
Ý Blood plates (platelets)

Fig. 16. Classification of blood formation elements

Erythrocytes A person is round bico-concave nuclear-free cells. They constitute the bulk of blood and determine its red color. The diameter of the erythrocytes is 7.2-7.5 microns, and the thickness is 2-2.5 μm. They have a big plasticity and easily pass on the capillars. As the erythrocytes agrees, their plasticity decreases. Erythrocytes are formed in the red bone marrow, where they ripen. In the process of ripening, they lose the kernel and only after that enter blood. They circulate in the blood for 130 days, and then destroy mainly in the liver and spleen.

In 1 μl of blood, men contain an average of 4.5-5 million erythrocytes, and in women -3.9-4.7 million. The number of erythrocytes does not constantly change in some physiological conditions (muscle work, when staying at large altitudes etc.).

The total surface of all erythrocytes of the adult is approximately 3,800 m 2, that is, 1500 times the surface of the body is 1500 times.

Erythrocytes contain respiratory pigment hemoglobin. In one erythrocyte there is about 400 million hemoglobin molecules. It consists of two parts: protein - globin and iron-containing - heme. Hemoglobin forms a fragile compound with oxygen - oxygemoglobin (NVO 2). At the same time, the compound the valence of iron does not change. 1 g of hemoglobin may be reduced by 1.34 ml o 2. Oxygemoglobin It has a bright-scarlet color, which determines the color of arterial blood. In the capillaries of tissues, oxymemoglobin is easily decomposed on hemoglobin and oxygen, which is absorbed by cells. Hemoglobin, who gave oxygen, is called restored hemoglobin (HB), it is it that determines the cherry blossom of venous blood. In the capillaries of tissues, hemoglobin connects with carbon dioxide, forming carboxygemoglobin. This compound falls into the lung capillaries, carbon dioxide diffuses alveoli into the air, from there, partially released into atmospheric air.

Hemoglobin is particularly easily connected with carbon monoxide CO, the resulting compound prevents the hemoglobin of oxygen to the hemoglobin, and as a result, the organism has severe consequences of oxygen starvation (vomiting, headache, loss of consciousness). Weak carbon monoxide poisoning are a reversible process: CO is gradually separated and output with fresh air.

The amount of hemoglobin in the blood has individual fluctuations and sexual differences: men are 135-140 g / l, in women - 125-130 g / l (Table 11).

The presence of a anemic state indicates a decrease in the number of erythrocytes (below 3 million) and the amount of hemoglobin is less than 60%. With anemia, either the number of erythrocytes can be reduced or the content of hemoglobin, or both in them. Most often occurs iron deficiency anemia. It may be due to the lack of iron in food (especially in children), impairment of iron absorption in the digestive tract or chronic blood loss (for example, with ulcerative disease, tumors, polyps, wrench invasion). Among other reasons are protein fasting, hypovitaminosis of ascorbic acid (vitamin C), folic acid, vitamins in 6, in 12, ecology.

The unfavorable living conditions of children and adolescents may lead to the emergence of Malokrovia. It is accompanied by headaches, dizziness, fainting, adversely affects the working capacity of students, the body's resistance is reduced, and children often sick.

Preventive actions:

Rational nutrition with a sufficient number of trace elements (Cu, Zn, CO, Mn, Mg, etc.) and vitamins (E, B 2, B 6, B 9, B 12 and folic acid);

Stay in the fresh air;

Rationing of educational, labor, motor activity and creative activity.

For newborn children, an increased hemoglobin content and a large number of red blood cells are characterized. The percentage of hemoglobin in the blood of children of the newborn period ranges from 100 to 140%, and the amount of erythrocytes may exceed 7 million in mm 3, which is associated with an insufficient supply of fetal oxygen in the last days of the embryonic period and during childbirth. After birth, gas exchange conditions are improved, part of the red blood cells decay, and the hemoglobin contained inside turns into a pigment bilirubin. The formation of large quantities of bilirubin can cause the so-called jaundice of newborns when the skin and mucous membranes are painted in yellow.

By 5-6 days, these indicators decrease, which is associated with the hematopoietic function of the brain.

Blood newborn contains a significant amount of unripe erythrocyte forms, there are erythrocytes containing the kernel (up to 600 in 1 mm 3 of blood). The presence of immature form of erythrocytes indicates the intensively flowing processes of blood formation after birth. Erythrocytes of newborns unequal sizes, their diameter ranges from 3.25 to 10.25 microns. After a month of life, only single nuclear erythrocytes meet in the child's blood.

By 3-4 years, the amount of hemoglobin and erythrocytes somewhat increases, in 6-7 years there is a slowdown in the increase in the number of erythrocytes and hemoglobin content, from 8 years of age, the number of erythrocytes and the amount of hemoglobin is repaired. In 12-14 years, an increase in the number of erythrocytes can be observed, usually to the upper boundaries of the norm, which is explained by the increased activity of the blood formation bodies under the influence of sex hormones during puberty. Sexual differences in blood hemoglobin are manifested in the fact that boys have a percentage of hemoglobin higher than girls.

Erythrocyte sedimentation rate (SE).When blood standing in a glass capillary, not coagulated due to the addition of anticularity substances, there is a gradual settlement of red blood cells. This is because the specific density of red blood cells is higher than plasma (1.096 and 1.027). The erythrocyte sedimentation rate depends on the ratio of albumin and globulins in the blood plasma. In addition, ESO is in linear dependence on the number of erythrocytes. The more erythrocytes, the slower they settle. EE is expressed in millimeters of plasma pillar's height over the layer of overvolored red blood cells per unit of time (usually in 1 hour).

In healthy women, the erythrocyte sedimentation rate varies within 2-15 mm / h, and men 1-10 mm / h in men. Usually, the speed of sedimentation of red blood cells in women is somewhat larger than in men. High ESO is observed in pregnant women (up to 45 mm / h), in the presence of inflammatory processes and with some other changes in the body. Therefore, SE is widely used as an important diagnostic indicator.

In newborns, the erythrocyte ethitocyte rate (from 1 to
2 mm / h). In children up to three years old, the value of SE varies from 2 to 17 mm / h. At the age of 7 and 12 years, the SE value does not exceed 12 mm / h.

Leukocytes belong to white (colorless) blood cells. They have a kernel and cytoplasm. The total number of leukocytes is less than the erythrocytes. In an adult, an adult before meals in 1 mm 3 contains 4000-9000 leukocytes. Their number is inconvenient, and it changes even during the day. An increase in the number of leukocytes is called leukocytosis, decrease - leukopenia.

Distinguish physiological and jet leukocytosis.

The first is observed after meals, during pregnancy, with muscle work, strong emotions, pain.

The second form is characteristic of inflammatory processes and infectious diseases. Reactive leukocytosis is due to an increase in cellular emission from blood formation organs with the predominance of young cell forms.

Lakeing It characterizes the flow of some infectious diseases (abdominal typhoid, flu, poliomyelitis, epidemic hepatitis, malaria). It is observed in the defeat of the red bone marrow as a result of irradiation.

There are three types of leukocytes: granulocytes, lymphocytes and monocytes.. Depending on whether the cytoplasma contains graininess or it is homogeneous, leukocytes are divided into two groups: granulocytes and agranulocytes.

Granulocytes. The name of these cells is associated with the presence of granules in their cytoplasm, detected by conventional methods of fixation and staining. Depending on the properties of granules, granulocytes are divided into neutrophilic(perceive both sour and main dyes), eosinophilic (painted with acidic paints) and finally basophilic (their cells are able to perceive the main paint). Granulocytes are 72% of all blood leukocytes (ATL., Fig. 3, p. 144), the time of their life is approximately 2 days.

The overwhelming majority of granulocytes are accounted for neutrophils. They are also called polymorphic nuclear, as they have a core of various shapes. In young neutrophils, the core is rounded, in young people - in the form of a horseshoe or wand (stickyuclear). With the age of cells, the kernel is rejected and divided into several segments, forming segmented neutrophils.

The time of finding neutrophils in the bloodstream is very small (on average 6-8 h), since these cells will quickly migrate into the mucous membranes. With acute infectious diseases, the number of neutrophils increases rapidly. They are able to receive energy by anaerobic glycolysis and therefore can even exist in poor oxygen tissues: inflamed, edema or poorly bloodsundhed. Neutrophists accumulate in places of damage to tissues or penetration of microbes, capture and digest them. In addition, neutrophils are isolated or adsorbed on its membrane antibodies against microbes and alien proteins.

Neutrophils are the most important functional elements of non-specific protection of the blood system, capable of neutralizing even such foreign bodies, with which the body has not previously met.

Eosinophila Possess the ability to phagocytosis. They contain large oval acidophilic granules consisting of amino acids, proteins and lipids. An increase in the number of eosinophils is called eosinophilia. Especially often, this condition is observed in allergic reactions, gliscate invasions and so-called autoimmune diseases, in which antibodies against their own cells are produced in the body.

Basophiles. 0.5-1% of all blood leukocytes (about 35 cells per 1 mm 3 are accounted for by basophils. The presence of these cells in the bloodstream is an average of 12 hours. Large granules in the cytoplasm produce heparin that prevents blood coagulation. In addition, The basophil membrane contains specific receptors to which certain blood globulines are joined. As a result of the formation of such an immune complex from the granules is released. histaminewhich causes the extension of the vessels, itching rash and in some cases the spasm of the bronchi.

Agranulocytes (end-in-law leukocytes). These cells are divided into lymphocytes and monocytes. (ATL., Fig. 2.3, p. 143-144). They account for 28% of all blood leukocytes, in children -50%. The formation of lymphocytes is many organs: lymph nodes, almonds, peers plaques, appendix, spleen, fork iron, bone marrow; The place of education of monocytes is the bone marrow. A condition in which the number of lymphocytes exceeds the usual level of their content, is called lymphocytosis, fall below normal size - lymphopenia.

All lymphocytes occur from stem lymphoid cells of the bone marrow, then they are transferred to the tissues where further differentiation are undergoing. At the same time, some lymphocytes develop and ripen in Timus, turning into T-lymphocyteswhich are later returned to the bloodstream. Other cells fall into the Fabrizian bag (Bursa) in birds or the lymphoid tissue of almonds, appendix, peer plaques of guts in mammals. Here they turn into mature In lymphocytes. After ripening, B-lymphocytes again go into the bloodstream and with it are spread to lymph nodes, spleen and other lymphoid formations.

The lymphocytes on the outer surface of the membrane have specific receptors that are able to be excited when meeting with alien proteins. At the same time, the T-lymphocytes through enzymes independently destroy these protein bodies: microbes, viruses, transplanted tissue cells. Because of this quality, they got a name killers - killer cells.

B-lymphocytes are somewhat differently reacting at a meeting with foreign bodies: they produce specific antibodies that are neutralized and associated with these substances, thereby preparing the process of their subsequent phagocytosis. Usually in the bloodstream is only part of lymphocytes, constantly turning into lymph and returning back (Recycling). Other lymphocytes are constantly localized in lymphoid fabric. During stressful states, lymphocytes are intensively destroyed under the influence of pituitary hormones and corticosteroids.

Lymphocytes are the central link of the immune system, as well as participate in cell growth processes, differentiation, tissue regeneration; Macromolecules of the information protein are transferred to control the genetic apparatus of other cells.

Monocytes. - the largest blood cells; They have a rounded shape with a well-pronounced cytoplasm. Monocytes accounted for 4% of all blood leukocytes. Monocytes are formed in bone marrow, lymph nodes, connective tissue. These cells have an amoebolic movement, are characterized by the highest phagocytic activity. The monocytes overlook the surrounding tissues; Here they grow and, reaching maturity, turn into fixed cells - gistocytes, or fabric macrophages. Near the inflammatory hearth, these cells can multiply by division.

There is a certain percentage of a certain percentage of leukocytes between certain types of leukocytes. leukocyte formula (Table 13)

Table. 13. Leukocyte formula (in%)

In infectious diseases, characteristic changes in the ratio of individual forms of leukocytes are observed. Acute bacterial infections are accompanied by neutrophilic leukocytosis and a decrease in the number of lymphocytes and eosinophils. In the future, the struggle against infection enters the stage of monocytosis; This is a sign of the victory of the body over pathogenic bacteria. Finally, the last stage of the fight against the pathogen agent is the stage of purification in which lymphocytes and eosinophils are involved. Chronic infectious diseases are accompanied by lymphocytosis. With tuberculosis, an increase in the number of lymphocytes often mark.

In the acute period of infectious disease, during the severe course of the disease, eosinophils may not be found in the blood, and with the beginning of recovery, even before visible signs of improving the condition of the patient, they are clearly visible under the microscope.

The most important function of leukocytes is the protection of the body from the microorganisms penetrating into the blood and tissue. All types of leukocytes are capable of an amoeboid movement, so that they can exit (migrate) through the wall of blood vessels. The speed of their movement can reach up to 40 microns / min. Leukocytes are capable of surrounding foreign bodies and capture them into the cytoplasm. The absorbed microorganism is destroyed and digested, leukocytes die, resulting in pus. This absorption of leukocytes in the organism of microbes is called phagocytosis(ATL., Fig. 5, p. 145). It was open to Russian scientists I. I. Mesnikov in 1882. One leukocyte can capture up to 15-20 bacteria. In addition, leukocytes allocate a number of substances important to protect the body. These include antibodies that have antibacterial and antitoxic properties, contributing to healing wounds. In the leukocytes of each type, certain enzymes contain certain enzymes, including proteases, peptidases, lipases, etc. Most (more than 50%) leukocytes are beyond the limits of the vascular bed, in the intercellular space, the rest (more than 30%) in the bone marrow.

The number of leukocytes and their ratio changes with age. In the newborn in the first 2 days there are more of them than in adults, and on average ranges from 10,000-20,000. Then the number of them begins to fall. Sometimes the second small rise between the 2nd and 9th day of life is noted. By the 7-12th day, the number of leukocytes decreases and reaches 10-12 thousand. Such a number of leukocytes remains in children of the first year of life, after which it decreases and by 13-15 years reaches the magnitude of the adult. The less the age of the child, the blood contains more immature forms of leukocytes. Leukocyte formula The child's blood during the newborn period is characterized by:

A consistent decrease in the number of lymphocytes from the moment of birth by the end of the newborn period (10 days);

A significant percentage of laughter forms and neutrophils;

The structural immaturity and fragility of leukocytes, so there are no segmented and rod forms, the kernels are loose and stained with lighter, the plasma of lymphocytes is often not painted.

By 5-6 years, the number of these uniform elements is aligned, after that the percentage of neutrophils is steadily growing, and the percentage of lymphocytes decreases (Table 14).

In children aged 3 to 7 years, neutrophil content is relatively low, and therefore the phagocytic function of blood is small. This can explain the exposure of preschool children with infectious diseases. Starting from 8-9 years, the phagocytic function of blood is enhanced, which significantly increases the body's resistance to the body.

Table. 14. The age characteristic of the leukocyte formula (in%)

Age (in years) Neutrophila Monocytes. Lymphocytes
1-2 34,5 11,5
4-5 45,5 9,0 44,5
6-7 46,5 9,5 42,0
7-8 44,5 9,0 45,0
8-9 49,5 8,5 39,5
9-10 51,5 8,0 38,5
10-11 50,0 9,5 36,0
11-12 52,5 9,0 36,0
12-13 53,5 8,5 35,0
13-14 56,5 8,5 32,0
14-15 60,5 9,0 28,0

The age fluctuations of the number of lymphocytes can be explained by the functional features of the blood formation organs: lymph nodes, spleen, bone marrow, etc. By 13-15 years, the components of the leukocyte formula reach the values \u200b\u200bof an adult.

Platelets and blood coagulation.Platelets, or blood plates, are independent cellular elements of the blood of an irregular round shape, surrounded by a membrane and usually devoid of kernels, with a diameter of 1-4 microns, a thickness of 0.5-0.75 μm. Blood plates are formed in the bone marrow (ATL., Fig. 4, p. 144). The ripening period of platelets is 8 days. They circulate in the blood for 5-11 days and then destroyed in the liver, lungs, spleen. The number of platelets in humans 200-400 × 10 9 / l (200,000-400,000 in 1 μl). The number of platelets increases with digestion, heavy muscle work (miogenic thrombocytosis), pregnancy. Daily fluctuations are occurring: thrombocyte during the night, than at night.

Platelet functions are diverse:

1) produce and excrete enzymes involved in blood coagulation;

2) have the ability to phagocytic nebiological foreign bodies, viruses and immune complexes involved in the non-specific protective system of the body;

Blood coagulation.Blood coagulation is of great biological significance, as it protects the body from a significant loss of blood.

All blood cells take part in blood coagulation (especially thrombocytes), proteins plasma (So-called blood coagulation factors), Ca +2 ions, vascular wall and surrounding vascular fabric. Normally, blood coagulation factors are in inactive state. Blood coagulation is a multistage process of enzymatic chain reactions that acts on the principle of feedback.

The blood coagulation process includes three phases.

Fig. 17. Scheme of blood coagulation process (by: Andreeva, 1998)

In the first phase, under the influence of external factors, the enzyme of the active promotinase is forming, in the second - the formation of the thrombin enzyme, in the third - the formation of fibrin fibrinogen. For the formation of Prothrombin in the liver, vitamin K is needed, and therefore the lack of this vitamin (for example, with a violation of the suction of fats in the intestine) leads to the blood coagulation disorders. The half-life of prothrombin from blood plasma is 1.5-3 days. Thromubin causes the transition of fibrinogen dissolved in the fibrin plasma, the threads of which form the basis of the thrombus. Such a bunch of blood closes a tight hole in the vessel and prevents further bleeding. The blood of a person extracted from the vascular bed is coagulated for 3-8 minutes. In some illnesses, this time may increase or decrease.

Blood coagulation hinders heparin - a substance that is produced by special cells - heparinocytes. Big accumulation is observed in lungs and liver. They are also located in the wall of blood vessels and a number of other fabrics. The coagulation is hampered by some substances formed in the body, the so-called antoslude factors.

Under normal conditions, the blood in the blood vessels is not coincided, but when damaged the inner shell of the vessel and in certain diseases of the cardiovascular system, it takes it to coagulation, while the bunch is formed in the blood vessel - thrombus.

The number of platelets in newborns fluctuates in fairly wide limits - from 150 to 350 thousand in 1 mm 3. In infants, the number of blood plates fluctuates on average from 230 to 250 thousand in 1 mm 3. With age, the content of platelets changes little. So, in children from 1 year to 16 years, the number of platelets fluctuates on average ranging from 200 to 300 thousand in 1 mm 3.

Children coagulation in the first days after birth slowdown, especially on the 2nd day of the child's life. From the 3rd to the 7th day of life, blood coagulation is accelerated and approaches the norm of adults. In children of preschool and school age, the time (or speed) of blood coagulation has broad individual fluctuations. On average, the start of coagulation in a drop of blood occurs after 1-2 minutes, the end of the coagulation - after 3-4 minutes.

Under a number of diseases (for example, when hemophilia) There is a lengthening of blood coagulation time, it can reach 30 minutes, sometimes several hours. The slowdown of blood coagulation depends on the lack of blood plasma antiamophilic globulinparticipating in the formation of thromboplastin. The disease is manifested in childhood exclusively in men; Hemophilia is inherited from a practically healthy woman from the family, one of whose members suffered from hemophilia. The disease is characterized by long bleeding due to injury or operational intervention. Hemorrhages can be in the skin, muscles, joints; There may be bleeding from the nose. Such children should avoid injury and be on dispensary accounting.

The blood maintains a relatively constant ratio of uniform elements.

In tab. 15 shows the hemogram of healthy children from 1 year to 15 years.

Table. 15. Hemogram of healthy children from 1 to 15 years
(Tour, Shabalov, 1970)

Age Erythrocytes 1: 10 6 in 1 μl Hemoglobin, g / l TROOMETS 1: 10 4 in 1 μl Leukocytes 1: 10 3 in 1 μl Soe, mm / h
M ± 0. M ± 0. M ± 0. M ± 0. M ± 0.
4,2 0,20 7,2 8,9 2,3
4,2 0,22 7,1 8,5 2,2
4,2 0,20 7,4 7,9 1,9
4,2 0,21 6,2 7,9 1,9
4,3 0,22 7,0 7,5 1,7
4,2 0,18 7,5 7,6 1,7
4,4 0,18 8,5 7,3 1,6
4,3 0,20 8,3 7,2 1,5
4,4 0,19 6,9 7,3 1,5
4,4 0,19 7,2 7,1 1,7
4,4 0,21 6,8 7,1 1,5
4,4 0,22 6,8 6,7 1,3
4,4 0,20 7,2 6,8 1,4
4,6 0,21 8,0 7,0 1,5

Immunity. Types of immunity.The protection of the body from alien substances is carried out by developing antibodies of various specificity, which can recognize all sorts of foreign substances.

Alien substance that causes the formation of antibodies is called antigen. By nature, the antigen is a highly molecular weight polymer of natural origin or a synthesized artificial way. The antigen consists of a large protein, polysaccharide or lipid molecule located on the surface of a microorganism or in free form.

In the process of evolution, the person has formed two immunity mechanisms - nonspecific and specific. Among that and the other allocate gumoral and cellular. Such a separation of the functions of the immune system is associated with the existence of two types of lymphocytes: T cells and B cells.

Nonspecific humoral immunity. The main role in this form of immunity belongs to protective substances of blood plasma, such as lysozyme, interferon. They provide congenital immunity of the body to infections.

Lizozyme It is a protein with enzymatic activity. It actively suppresses the growth and development of causative agents of disease, destroys some bacteria. Lizozyme is contained in intestinal and nasal mucus, saliva, tear fluid.

Interferon - blood plasma globulin. It is quickly synthesized and released. It has a wide range of action and provides antiviral protection before increasing the number of specific antibodies.

Nonspecific cellular immunity. This type of immunity is determined. phagocytic activity granulocytes, monocytes, platelets. Granulocytes and monocytes contain a large number of lysosomal enzymes, and their phagocytic activity is most pronounced. In this reaction, several stages are distinguished: the addition of phagocyte to the microbe, the absorption of the microbe, its enzymatic digestion and removal of the material remaining not destroyed.

Specific cell immunity. Here the main role is played by T-lymphocytes, which ripen in the forged gland and enter the bloodstream. T-cells are constantly overlooking the thymus and enter the lymph nodes and the spleen, where in the event of a meeting with a specific antigen recognize it and begin to share. One part of the subsidiary
T-lymphocytes associated with an antigen and destroys it. T-lymphocytes can attack alien cells due to the specific receptor for the antigen embedded in the plasma membrane. This reaction occurs with the participation of special T-helper cells (assistants). Another part of the daughter lymphocytes is the so-called T-cells with immunological memory. They "remember" an antigen from the first meeting with him and "recognize" when repeated contact. This identification is accompanied by intense division, forming a large number of effector T-lymphocytes - killer cells.

Specific humoral immunity. This type of immunity is created in lymphocytes of lymph nodes, lipids and other lymphatic authorities. At the first meeting with an antigen in lymphocytes, it is started to divide and differentiate, forming plasma cells and memory cells. Plasma cells produce and isolated in blood plasma. Humoral antibodies. And here in the development of antibodies T-helpers participate. Repeated