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[嗜热放线菌硫醇依赖性丝氨酸蛋白酶的体外纤溶和溶栓特性]

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

作者信息

Rudenskaia G N, Liutova L V, Andreenko G V, Karabasova M A, Tsaplina I A

出版信息

Prikl Biokhim Mikrobiol. 1987 Nov-Dec;23(6):754-61.

PMID:3481858
Abstract

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.

摘要

研究了类枯草杆菌蛋白酶样硫醇依赖性丝氨酸蛋白酶的纤溶和溶栓特性。在浓度为50至4000微克/毫升时,该酶可导致纤维蛋白平板溶解并激活纤溶酶原。在浓度高于100微克/毫升时,它对由血浆以及人和大鼠血液在体外形成的凝块显示出明显的溶栓作用。血浆抑制剂可部分使硫醇依赖性丝氨酸蛋白酶失活。该酶还可水解纤维蛋白原、凝血酶、纤溶酶和纤溶酶原。

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