蚯蚓纤溶酶新组分的分离纯化及部分性质  

Purifi cation and Partial Properties of New Components of Earthworm Fibrinolytic Enzymes

作　　者：武金霞[1] 张贺迎[2] 赵晓瑜[2] 杜学敏[3] 

机构地区：[1]河北大学生命科学学院 [2]河北大学生物工程研究中心,河北保定071002 [3]石家庄医学高等专科学校,河北石家庄050071

出　　处：《中国医药工业杂志》2008年第6期420-422,共3页Chinese Journal of Pharmaceuticals

基　　金：河北省自然科学基金项目(C2005000118)

摘　　要：采用以大豆胰蛋白酶抑制剂为配基的亲和色谱分离蚯蚓纤溶酶,以DEAE-纤维素-52离子交换柱色谱和制备电泳纯化各单组分。结果表明新组分8、9、10都是能水解纤维蛋白的糖蛋白。组分8是一种纤溶酶原激活剂,有2个亚基,Mr为25.5k和17.8k;组分9仅一条肽链,Mr为33.6k;组分10含有Mr为18.7k和10.9k的2个亚基。组分9、10均兼有纤溶酶原激活活性和直接纤溶活性。Earthworm fibrinolytic enzyme components were separated by affinity chromatography with soybean trypsin inhibitor as ligand. Single components were purified through DEAE-cellulose-52 chromatography and preparative electrophoresis. New components 8, 9 and 10 are all glycoproteins capable of hydrolyzing fibrin. Component 8 is a plasminogen activator consisting of two subunits of 25.5k and 17.8k. Component 9 is only one polypeptide of 33.6k, and component 10 contains two subunits of 18.7k and 10.9k. Both component 9 and 10 showed plasminogen-activating and fibrinolytic activities.

关 键 词：蚯蚓纤溶酶 纤溶酶原激活剂 糖蛋白 分离纯化 

分 类 号：Q513.2[生物学—生物化学] Q556.3