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Our study of 820 microorganisms from various systematic and ecological groups revealed that 72% of the cultures contained enzymes caoable to dissolve human fibrin clots in vitro. Fibrinolytic enzymes are formed during growth of producers on strictly specific media. Changes in the composition of media and conditions of enzymatic synthesis were found to increase the specificity of microbial proteases to fibrin and to decrease their sensitivity to fibrinolytic enzymes inhibitors. A thrombolytic enzyme (TE) has been isolated and purified from the cultural fluid of actinomycetes. An intravenous injection of TE to albino rats results in an increase of fibrinolytic activity of the blood plasma euglobulin fraction. Time of euglobulin clot lysis is thereby decreased by 32%. The fibrinolytic activity measured from euglobulin precipitate on un-heated fibrin plates is increased 2.3-fold. However, the fibrinolytic activity of non-diluted blood plasma remains unchanged probably due to a sharp rise in antiplasmin content following TE injection. TE exerts marked thrombolytic effect in vivo. After intravenous injection of TE to animals with artificial clots in a v.jugularis segment a rapid clot lysis and reconstitution of blood flow are observed.

Blood coagulation, fibrinolysis in plasma and peritoneal fluid, and activity of tissue plasminogen activator in the peritoneum and uterine horns were studied in albino rats after surgery on the uterine horns with a monopolar electrical scalpel. This instrument induced severe inflammatory reaction and disturbances in the fibrinolysis and coagulation systems.