Purification and Characterization of Jerdonitin, a Non-hemorrhagic Metalloproteinase from Trimeresurus jerdonii Venom  

菜花烙铁头蛇毒金属蛋白酶Jerdonitin的分离纯化和理化性质(英文)

作　　者：陈润强[1] 金扬[1] 吴健波[1] 钟树荣[1] 朱绍文[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》2005年第6期616-621,共6页动物学研究（英文）

基　　金：ThisworkwassupportedbyNaturalScienceFoundationofYunnanScienceandTechnologyCommittee(2002C0063M)

摘　　要：Previously, we have purified Jerdonitin from Trimeresurusjerdonii venom. Compared with other P-Ⅱ class snake venom metalloproteinases （SVMPs）, Jerdonitin has a primary structure comprising metalloproteinase and disintegrin domains. However, no hemorrhagic and fibrinogenolytic activities were detected for Jerdonitin. We thought that organic buffer of high performance liquid charamatography （HPLC） might affect its enzymatic activity. In this study, we purified Jerdonitin by another procedure excluding the HPLC. It was homogenous as judged by SDS-PAGE and had an apparent molecular weight of 36 kDa under non-reducing conditions and 38 kDa under reducing conditions, respectively. Like other typical metalloproteinases, Jerdonitin preferentially degraded alpha-chain of human fibrinogen and this fibrinogenolytic activity was completely inhibited by EDTA, but not by PMSF. It was interesting that Jerdonitin did not induce hemorrhage after intradermal injection in mice.以前从菜花烙铁头蛇毒中分离纯化到Jerdonitin。与其他Ⅱ型蛇毒金属蛋白酶相比,Jerdonitin由金属蛋白酶和去整合素两个结构域组成。但没有检测到其出血和纤维蛋白原降解活性,推测可能高压液相色谱的有机溶液影响了其酶活性。采用不含高压液相色谱柱层析的新分离手段分离得到Jerdonitin。Jerdonitin在还原和非还原SDS-PAGE电泳中分别呈现一条表观分子量为38和36kDa的条带。像其他典型的蛇毒金属蛋白酶一样,Jerdonitin优先降解人纤维蛋白原的alpha链,并且该活性能被EDTA完全抑制,而PMSF对其没有影响。Jer-donitin不诱导小白鼠皮下出血。

关 键 词：Trimeresurus jerdonii SVMP HEMORRHAGE Fibrinogenolytic activity 

分 类 号：Q55[生物学—生物化学]