江浙蝮蛇毒精氨酸酯酶Agkihpin的研究 Ⅰ.分离纯化和初步表征  

Research on Arginine Esterase from Crude Venom of Gloydius brevicaudus(Stejneger) I.Purification and Characterization

作　　者：胡启平[1] 舒雨雁[2] 

机构地区：[1]广西医科大学细胞生物学与遗传学教研室,南宁530021 [2]广西医科大学蛇毒研究所

出　　处：《四川动物》2006年第2期251-256,F0003,共7页Sichuan Journal of Zoology

基　　金：国家自然科学基金资助(No.39970174)

摘　　要：江浙蝮蛇毒中存在有多种精氨酸酯酶,其中有多种已被纯化,本研究应用离子交换和凝胶过滤等方法,新分离纯化了一种精氨酸酯酶,命名为Agkihpin,分子量约为25·46KDa,等电点约为7·43,含235个氨基酸残基,糖蛋白染色阴性,是单链蛋白,对TAME的最适pH为8·2。There are a few kinds of arginine esterase in the venom of Gloydius brevicauclus （Stejneger）, in which some kinds of arginine esterase have being purified. In this research, a new arginine esterase was purified from the venom of Agkistrodon halys Pallas by ion exchange and gel filtration, named Agkihpin. Agkihpin is a single-strand protein, no glycoprotein, containing 235 amino acid residues, with a molecular weight of 25. 46 kDa and an isoelectric point of 7.43, and possessing an optimum pH 8.2 to TAME.

关 键 词：江浙蝮蛇 蛇毒 精氨酸酯酶 分离纯化 

分 类 号：Q55[生物学—生物化学]