竹叶青蛇毒丝氨酸蛋白酶杰多纤溶酶的纯化与特性研究

Purification and characterization of jerdofibrase, a serine protease from the venom of Trimeresurus jerdonii snake.

作者信息

Jin Y, Lu Q M, Wei J F, Li D S, Wang W Y, Xiong Y L

机构信息

Department of Animal Toxinology, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China.

出版信息

Toxicon. 2001 Aug;39(8):1203-10. doi: 10.1016/s0041-0101(00)00261-0.

DOI:10.1016/s0041-0101(00)00261-0

PMID:11306131

Abstract

A fibrin(ogen)olytic serine protease from Trimeresurus jerdonii venom was identified and purified to SDS-polyacrylamide gel electrophoresis homogeneity. It is a single chain polypeptide with a molecular weight of 32kDa under reduced condition and 28kDa under non-reduced condition, respectively. The venom protease catalysed the hydrolysis of some chromogenic substrates such as S2238, S2160, S2302 and S2251. It degraded Bbeta-chain of human fibrinogen preferentially. Also the enzyme degraded fibrin directly. Its enzymatic activity was completely inhibited by phenylmethylsulfonyl fluoride (PMSF), but not affected by EDTA. That suggested it was a serine protease. N-terminal sequence of the purified component showed high homology with other snake venom serine proteases.

摘要

从竹叶青蛇毒中鉴定并纯化出一种纤维蛋白（原）溶解丝氨酸蛋白酶，使其达到十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳均一性。它是一种单链多肽，在还原条件下分子量为32kDa，在非还原条件下分子量分别为28kDa。该蛇毒蛋白酶催化一些发色底物如S2238、S2160、S2302和S2251的水解。它优先降解人纤维蛋白原的Bβ链。此外，该酶还直接降解纤维蛋白。其酶活性被苯甲基磺酰氟（PMSF）完全抑制，但不受乙二胺四乙酸（EDTA）影响。这表明它是一种丝氨酸蛋白酶。纯化组分的N端序列与其他蛇毒丝氨酸蛋白酶具有高度同源性。