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Biomedical subjects

G V Andreenko

Publications and source records attributed to G V Andreenko.

At least 145 records · Page 8Linked to original sources

[Interleukin-1 and fibrinolysis. In vivo studies].

Distinct decrease in fibrinolytic activity of both whole blood plasma and its euglobulin fraction, occurring due to liberation of an inhibitor of plasminogen activator into circulation, was observed within 2-4 hrs after a single intravenous administration of rabbit interleukin-I into rats at a dose of 50 micrograms/kg, while the activator activity was increased in kidney heart, spleen and lung tissues. The similar data were obtained if the dose was either increased up to 150 micrograms/kg or decreased down to 5 micrograms/kg and 0.5 micrograms/kg, but the effect observed proved to be dose-dependent. Three injections of interleukin-I caused more pronounced increase in concentration of fibrinogen and antiplasmins as compared with controls.

Animals↗

[Isolation and properties of acylplasmin].

Plasmin, free of an activator, was obtained after activation of the highly purified human plasminogen by means of trypsin immobilized on Sepharose 4B and after removal of the enzyme from the system. Plasmin was acylated at the active centre using p-amidinophenyl ester of p'-anisic acid to produce the fibrinolytic agent causing a long-term effect. Inactive acyl plasmin was deacylated with the constant rate k3 = 3.10(-4) c-1 (r1/2 = 40 min) at pH 7.4 and 37 degrees. Preliminary studies of the anisoyl-plasmin effect on the system of fibrinolysis in rats showed that in the absence of fibrin clot the fibrinolytic activity was not increased immediately in the euglobulin fraction of blood but after 30 min in result of deacylation of the acyl-enzyme administered into circulation.

Animals↗

[Thrombolytic properties of the heparin-tissue plasminogen activator complex and its effect on the fibrinolytic and coagulating systems of the blood in animals].

A complex heparin-tissue activator of plasminogen maintain its thrombolytic properties due to the presence of the activator. Studies of thrombolytic properties of the complex in vitro and of its effect in vivo on animal blood fibrinolytic and coagulation systems after intravenous administration confirmed this contention. After intravenous administration into animals the complex caused only slight effect on the system of fibrinolysis and inhibited moderately the coagulating activity of blood. This combination of heparin and tissue activator of plasminogen appears to be important in treatment of thromboses.

Animals↗

[Determination of the plasminogen level in rat plasma].

Content of plasminogen was estimated in rat blood plasma using streptokinase and human blood euglobulin fraction in order to activate plasminogen. By means of the procedure described the content of plasminogen was evaluated in blood of healthy animals and of the animals treated with tissue activator of plasminogen from pig heart.

Animals↗

[The role of fibrinolytic system in pneumonias complicated by exudative pleurisy in children].

Phasic alterations in fibrinolytic activity were found in blood plasma of children with pneumonia complicated by exudative pleurisy. Hypercoagulation and inhibition of fibrinolytic activity were observed at the beginning of the disease. Hypercoagulation and an increase in the fibrinolytic activity occurred during restoration. In the children with lung destruction the fibrinolytic activity was increased in blood and in exudates before the appearance of roentgenologic indications of the destructive alterations. The fibrinolytic activity was inhibited in children with metapneumonic pleurisy formed during pneumonia and characterized by long-term and severe course. Role of fibrinolysis as possible pathogenetic factor responsible for development of complications is discussed.

Blood Coagulation Tests↗

[Fibrinolytic and thrombolytic properties of thiol-dependent serine proteinase from Thermoactinomyces vulgaris in vitro].

Fibrinolytic and thrombolytic properties of the subtilisin-like thiol-dependent serine proteinase were studied. At concentrations from 50 to 4000 micrograms/ml the enzyme causes lysis of fibrin plates and activates plasminogen. At concentrations above 100 micrograms/ml it shows a pronounced thrombolytic effect on the clots formed in vitro from both plasma and human and rat blood. Plasma inhibitors partly inactivate the thiol-dependent serine proteinase. The enzyme hydrolyses also fibrinogen, thrombin, plasmin and plasminogen.

Actinomyces↗

[Effect of diets with a varying protein content on fibrinolysis in ischemic heart disease].

A comparative influence of an antiatherosclerotic diet with a reduced proportion of protein (65--70 g) and of a diet with an amount of protein in line with the physiological standard (100--110 g) on the fibrinolysis and lipids spectrum of the blood was studied in 60 patients with ischemic heart disease. The antiatherosclerotic diet is shown to have most favourable effect both on the fibrinolytic system and on the lipids metabolism with the protein proportion of 100--110 g, i.e. in keeping with the physiological standards. A reduction of the protein content in the diet of patients with ischemic heart disease lowers the effect of treatment and does not have any positive influence on the function of the fibrinolytic system.

Adult↗

[Stability of tissue plasminogen activator].

Stability of the tissue activator plasminogen was studied in various experimental conditions in vitro. The enzyme did not loss its activity after 3 hrs incubation and 7-fold dilution with physiological saline. Blood plasma, added to the tissue activator plasminogen preparation, decreased twice the enzyme activity even without preincubation. In blood plasma, obtained within 1 min after intravenous administration of the activator preparation, inhibition of the enzyme occurred during all the period of incubation and it was more pronounced.

Animals↗