来自罗素蝰蛇（Vipera russelli）毒液的一种蛋白酶与蛋白酶抑制剂的协同相互作用。

Synergistic interaction of a protease and protease inhibitors from Russell's viper (Vipera russelli) venom.

作者信息

Jayanthi G P, Gowda T V

机构信息

Department of Biochemistry, University of Mysore, Manasagangotri, India.

出版信息

Toxicon. 1990;28(1):65-74. doi: 10.1016/0041-0101(90)90007-t.

DOI:10.1016/0041-0101(90)90007-t

PMID:2184544

Abstract

An acidic proteolytic enzyme, RVVX, was purified from Vipera russelli venom by successive chromatography on CM-Sephadex C-25, DEAE-cellulose and Sephadex G-100 columns. RVVX is a glycoprotein with a mol. wt of 79,000. It exhibited caseinolytic and factor X activating properties. Two trypsin inhibitors, TI-I and TI-II, were purified from V. russelli venom in a single step by CM-Sephadex C-25 column chromatography. The trypsin inhibitors interacted with the proteolytic enzyme RVVX. TI-I inhibited only the factor X activating property of RVVX while TI-II inhibited both, the caseinolytic and also factor X activating properties of RVVX. The edema inducing activity of RVVX increased markedly in the presence of non-edema inducing doses of TI-I and TI-II. RVVX, TI-I and TI-II were non-lethal in mice. The combination of RVVX and TI-II demonstrated enhanced toxicity.

摘要

一种酸性蛋白水解酶RVVX，通过在CM - Sephadex C - 25、DEAE - 纤维素和Sephadex G - 100柱上连续色谱法从圆斑蝰蛇毒中纯化得到。RVVX是一种分子量为79,000的糖蛋白。它具有酪蛋白水解活性和激活因子X的特性。两种胰蛋白酶抑制剂TI - I和TI - II，通过CM - Sephadex C - 25柱色谱法一步从圆斑蝰蛇毒中纯化得到。这些胰蛋白酶抑制剂与蛋白水解酶RVVX相互作用。TI - I仅抑制RVVX的因子X激活特性，而TI - II则同时抑制RVVX的酪蛋白水解活性和因子X激活特性。在非致水肿剂量的TI - I和TI - II存在下，RVVX的致水肿活性显著增加。RVVX、TI - I和TI - II对小鼠无致死性。RVVX与TI - II的组合表现出增强的毒性。