STRUCTURE-FUNCTION FEATURES AND EFFECTS ON BLOOD COAGULATION OF SNAKE VENOM SERINE PROTEASES*  

蛇毒丝氨酸蛋白酶结构与功能特性及其对血液凝固系统的作用(英文)

作　　者：张云[1] 李文辉[1] 高荣[1] 吕秋敏[1] 王婉瑜[1] 熊郁良[1] 

机构地区：[1]中国科学院昆明动物研究所动物毒素研究室

出　　处：《Zoological Research》1998年第2期97-106,共10页动物学研究（英文）

基　　金：国家自然科学基金;云南省后备人才培养基金;中国科学院"九五"青年基金

摘　　要：Snake venoms,especially those from the two subfamilies,Crotalinae and Viperinae,contained a lot of serine proteases. They were responsible for the hemorrhage,shock,or disorder of blood coagulation after envenomation. They acted,by activating,inactivating,or other converting effects,on almost all the components of hemostatic and fibrinolytic systems. Their sequences were homologous to trypsin-kallikrein serine proteases. Variation of primary sequences out of active center results in the difference of substrate specificities and the further difference of biological and pharmacological activities. Because of their common and unique properties compared to their physiological corresponding factors,snake venom proteases are proved to be an excellent model for the study of protease substrate discriminating mechanism. Furthermore,they have found an important position both in basic research and application of hemostasis and thrombosis in clinic.蛇毒，特别是蝰亚科（Ｃｒｏｔａｌｉｎａｅ）和腹亚科（Ｖｉｐｅｒｉｎａｅ）蛇毒，含有大量丝氨酸蛋白酶。这是自然界长期进化过程中演化出的一类既和哺乳动物蛋白酶相似，又存在相当程度的结构与功能分化的生物大分子，通过激活、灭活和转变机体中的凝血因子而广泛作用于血液凝固系统。它们的一级序列和胰蛋白酶——激肽释放酶同源。它们具有相同的活性中心构造和酶催化机制，但活性中心外可变区序列的差异造成了它们底物专一性差异，进一步体现为生物学和药理学功能的差异。它们和哺乳动物生理同功酶比较，由于其共性及特性，蛇毒丝氨酸蛋白酶成为蛋白酶底物识别问题探讨研究的优良模型，并在临床医学诊断及心血管疾病治疗中得到广泛应用。

关 键 词：VENOMS Proteases Blood coagulation 

分 类 号：Q55[生物学—生物化学] Q592