来自黎凡特蝰蛇（蛇）毒液的一种蛋白酶的纯化及特性

Purification and properties of a proteinase from Vipera lebetina (snake) venom.

作者信息

Mähar A, Siigur E, Siigur J

出版信息

Biochim Biophys Acta. 1987 Sep 11;925(3):272-81. doi: 10.1016/0304-4165(87)90192-9.

Abstract

A proteinase from the venom of Vipera lebetina was purified by chromatography on Sephadex G-100 and CM-cellulose. The purified proteinase was homogeneous on SDS-polyacrylamide gel electrophoresis and consisted of a single chain with molecular weight of 37,000 +/- 1500. The isoelectric point of the proteinase was over 10. The enzyme was active on casein but not on esters and amides of arginine. It split the oxidized insulin B-chain at the peptide bonds of Tyr16-Leu17, Phe24-Phe25 and Phe25-Tyr26, and glucagon at the bonds Tyr10-Ser11, Leu14-Asp15 and Leu26-Met27. The enzyme was inhibited by DFP and PMSF, and partially by soybean trypsin inhibitor, but not with EDTA.

摘要

通过在葡聚糖G - 100和CM - 纤维素上进行色谱分离，从黎凡特蝰蛇毒液中纯化出一种蛋白酶。纯化后的蛋白酶在SDS - 聚丙烯酰胺凝胶电泳上呈现均一性，由一条分子量为37000±1500的单链组成。该蛋白酶的等电点超过10。该酶对酪蛋白有活性，但对精氨酸的酯类和酰胺类无活性。它在氧化胰岛素B链的Tyr16 - Leu17、Phe24 - Phe25和Phe25 - Tyr26肽键处裂解，在胰高血糖素的Tyr10 - Ser11、Leu14 - Asp15和Leu26 - Met27键处裂解。该酶被DFP和PMSF抑制，并被大豆胰蛋白酶抑制剂部分抑制，但不被EDTA抑制。