基因重组蛇毒纤溶因子rFII的酶学特性研究  

Studies on Enzyme Characteristics of Recombinant Fibrinolytic Enzyme of Agkistrodon acutus Venom

作　　者：江伟健[1] 邱鹏新[1] 颜光美[1] 

机构地区：[1]中山大学基础医学院药理学教研室,广州510080

出　　处：《热带医学杂志》2005年第4期413-415,共3页Journal of Tropical Medicine

基　　金：广东省科技计划资助项目(No.2003A10905)

摘　　要：目的研究重组蛇毒纤溶因子的酶学特性。方法通过SDS-PAGE分析其分子量、纯度,用SDS-PAGE方法检测其对纤维蛋白原的水解能力,用分光光度法检测其水解azocasein的能力和PMSF及EDTA对蛇毒纤溶因子的作用。结果蛇毒重组纤溶因子rFII是一个分子量在28000的蛋白酶。它呈时间和浓度依赖性水解纤维蛋白原的Aα、Bβ、γ亚基,EDTA和PMSF均可以抑制该因子水解azocasein的能力。结论rFII是一种纤维蛋白原酶,它的酶活性可同时被EDTA和PMSF所抑制。Objective To characterize the recombinant fibrinolytic enzyme (rFII) of Agkistrodon acutus Venom. Methods The molecular weight and fibrinogenolytic activity were determinaed by SDS-PAGE. Azocasein was used as substrate to investigate the caseinolytic activity and the effects of EDTA and PMSF on rFII. Results rFII is a proteinase with a molecular weight of 28000. It acted on the Aα, Bβ,γ chain of fibrinogen directly. The caseinolytic activity was inhibited by EDTA and PMSF. Conclusions rFII is a recombinant proteinase which can hydrolyze fibrinogen. The enzymatic activity can be inhibited by EDTA and PMSF.

关 键 词：蛇毒 尖吻蝮蛇 纤维蛋白原 蛋白酶 EDTA PMSF 

分 类 号：Q959.6[生物学—动物学] Q55