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Biomedical subjects

V A Protsenko

Publications and source records attributed to V A Protsenko.

At least 73 records · Page 4Linked to original sources
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[Quantitative characteristics of serum antitryptic activity].

The method suggested includes incubation of trypsin with native blood serum and subsequent quantitative determination of trypsin, that did not react with inhibitor, by means of the antitryptic precipitating serum. The method is based on the principle of radial immunodiffusion. In native serum that was not subjected to dilution the antitryptic capacity is 210.0 +/- 27.3 microng/ml in people, 238.7 +/- 33.1 microng/ml in rabbits. A distinct dynamics of changes in the antitryptic capacity of blood serum is observed with experimental hypertrypsinemia.

Animals↗
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[Effect of kontrikal on the activity of proteolytic enzymes and their inhibitors in blood, state of the bronchoalveolar secretion and the nature of the lung damage in dysenteric intoxication].

The development of dysenteric intoxication in rabbits led to an abrupt increase in the blood activity of proteolytic enzymes. This increase was accompanied by the reduced content of alpha 1-antitrypsin, and that of rapid and slow kallikrein inhibitor. Meanwhile there occurred a remarkable decrease in blood serum ability to bind chymotrypsin and kallikrein, and diminution of alpha 2-macroglobulin level. Trypsin, binding by blood serum did not undergo any substantial changes. In these conditions, the permeability of pulmonary vessels drastically rose and surface activity of the washing off dropped. The pathomorphological alterations in the lungs corresponded with the appearance of the "shock lung". Contrykal normalized the blood content of proteolytic enzymes and inhibitors, as well as that of the bronchoalveolar washing off, averted the development of gross pathomorphological alterations, exerting no appreciable effect on the surface activity of the bronchoalveolar washing off.

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[Levels of alpha 1-antitrypsin and alpha 2-macroglobulin in blood serum and its antitryptic capacity].

Immunochemical analysis in combination with gel filtration and isoelectric focusing made it possible to state that in blood serum of healthy people 81.3 +/- 0.5% of administered trypsin is bound with alpha 1-antitrypsin and 18.7 +/- 0.6%--with alpha 2-macroglobulin. The latter is functionally heterogeneous, only 40% of it is bound with trypsin and in the formed complex the antigenic properties of trypsin and alpha 2-macroglobulin are lost. A great number of blood serum alpha 1-antitrypsin cannot fix trypsin. The content of such alpha 1-antitrypsin rises sharply with pathology available. In the immunochemical estimation of the organism inhibitory potential relative to proteolytic enzymes not only the amount of the inhibitor but also its functional activity should be taken into account. The data of immunochemical research of the blood serum isoelectrophoregrams show that the most considerable changes under conditions of pathology occur in alpha 2-macroglobulin.

Humans↗
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[Origin of tissue basophils and basophilic granulocytes of the blood].

The paper deals with analysis of modern literature on origin of basophils and basophilic blood granulocytes. Data of radioimmunologic, electron-microscopic, cytochemical and morphological studies make it possible to conclude that these cells are of bonemarrow origin.

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[Effect of proteolytic enzyme inhibitors on lung cell population function in normal mice and in the development of tourniquet shock].

Cell populations of mice lungs have been studied for variations in the lavage and lumen of the alveoli. The development of the tourniquet shock induces a decrease in the number of macrophages and lymphocyte and an increase in the number of neutrophils, erythrocytes and epithelium cells. Application of the proteolysis enzyme inhibitors is found to stabilize the bronchoalveolar barrier and to prevent these changes.

Animals↗
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[Proteolytic enzyme inhibitor and the kinin system in thyrotoxicosis].

Free bradykinin, kininogen, kininase, protease inhibitors of alpha 1-antitrypsin, alpha 1-antichymotrypsin, alpha 2-macroglobulin, and antitryptic volume of the blood serum were examined in 25 patients suffering from goiter with thyrotoxicosis symptoms. Activation of the kinin system and reduction in the antitryptic volume were revealed before the operation. The level of the rest inhibitors was elevated. After operative intervention these changes became more expressed. alpha 2-Macroglobulin content increased. By the moment of discharge the above parameters tended to normalization. The content of the majority of inhibitors, however, did not reach normal. This should be taken into consideration during rehabilitation of patients with thyrotoxicosis.

Adult↗
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[Effect of proteolysis enzymes and their inhibitors on oxygen uptake by rat brain tissue and its antitryptic activity].

Trypsin in a dose of 3 microgram increases the intensity of oxygen uptake and antitryptic capacity of the brain tissue in animals under study. These indices decrease considerably under the effect of trypsin in a dose of 6-12 microgram. Kallikrein in the same doses has a unidirected stimulating effect. The antitryptic serum and ingitryl block the biological effect of trypsin and similarly to the rabbit normal and antikallikreinic serum stimulate the oxygen uptake.

Animals↗
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[Effect of proteolysis inhibitors on serum proteinase activity and its antitryptic activity in postischemic toxemia].

Parenteral administration to animals of the antikallikrein serum containing 200gamma/ml of antibodies to the pancreatic kallikrein (10 ml/kg), ingitryl (1.5 Un/kg) and of tracilol (10 000 Un/kg) exerts in post-ischemic toxemia an inhibiting effect on the protamine-splitting blood serum activity and does not affect the benzoylarginine-paranitroanilide rate of splitting. Changes of the blood serum ability to bind trypsin and manifestation of the protamine-splitting activity during the first 9 hours of observation are of an undulating nature and the changes of these characteristics are reciprocal.

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[Serum antiprotease activity following parenteral administration of proteolytic enzymes, histamine and acetylcholine].

State of tryptic and antienzymatic activities of rabbit blood serum was studied after parenteral administration of trypsin, chymotrypsin, histamine, acetylcholine and kallikrein. Treatment with chymotrypsine led to the most favorable alterations in animals as compared with trypsin and kallikrein effects. Activity of trypsin was increased and the antienzymatic activity was decreased in blood serum after administration of histamine and acetylcholine. This suggests that antiprotease drugs may be used in therapy of diseases, accompanied by increase in content of histamine and acetylcholine.

Acetylcholine↗
PubMedDate not supplied

[Immunochemical assessment of the antigenic relationship between the pancreatic kallikrein of rodents and carnivores].

Using quantitative and qualitative immunochemical methods, in combination with isoelectrical focusing, it was shown that antibodies to commercial kallikrein are involved into precipitation reaction with kallikrein in extracts from the pancreas of dogs, cats, guinea pigs, rats and mice. Complexes antigen--antibody exhibit similar physico-chemical properties; during isoelectric focusing, they are found in the same pH range as the immunoactive portion of commercial kallikrein. These data indicate antigenic similarity of pancreatic kallikrein in different mammalian species.

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