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Characteristics and Properties of the Complex of Proteolytic Enzymes of the Thrombolytic Action of the Micromycete Sarocladium strictum
Applied Biochemistry and Microbiology ( IF 0.8 ) Pub Date : 2021-02-24 , DOI: 10.1134/s0003683821010129
E. I. Kornienko , A. A. Osmolovskiy , V. G. Kreyer , N. A. Baranova , I. B. Kotova , N. S. Egorov

Abstract

A preparation of thrombolytic enzymes of micromycete S. strictum 203 was obtained and characterized. The expressed urokinase activity of producer proteinases was determined, and the content of the complex of three alkaline trypsin-like thiol-dependent serine-type proteinases with different isoelectric points (4.5, 7.2 and 11.8) but close molecular weight was detected in the enzyme preparation (about 35 kDa). One of the proteinases (proteinase III) was not glycosylated, and the rest were glycoproteins. The proteinases differed in the spectrum of proteolytic activity in relation to proteins; the thrombus components also turned out to be different. Presumably, the enzymatic urokinase activity causes proteinases to activate plasminogen.



中文翻译:

缩孔霉菌沙门氏菌溶栓作用蛋白水解酶复合物的特性和性能

摘要

micromycete的血栓溶解酶的制备S. strictum获得和表征203。确定生产者蛋白酶表达的尿激酶活性,并测定三种碱性胰蛋白酶样硫醇依赖性丝氨酸型蛋白酶(等电点不同(4.5、7.2和11.8),但分子量接近)中复合物的含量(约35 kDa)。一种蛋白酶(蛋白酶III)未糖基化,其余为糖蛋白。蛋白酶在蛋白水解活性方面与蛋白质有关;血栓成分也有所不同。据推测,酶促尿激酶活性导致蛋白酶激活纤溶酶原。

更新日期:2021-02-24
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