[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.
D000190:Actinomyces / Q000201:enzymology*; D001780:Blood Coagulation Tests; D005343:Fibrinolytic Agents / Q000302:isolation & purification; D006801:Humans; D066298:In Vitro Techniques; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D013438:Sulfhydryl Compounds
D005343:Fibrinolytic Agents; D013438:Sulfhydryl Compounds; D012697:Serine Endopeptidases
Issledovanie fibrinoliticheskikh i tromboliticheskikh svoĭstv tiolzavisimoĭ serinovoĭ proteinazy iz Thermoactinomyces vulgaris in vitro.