产芽孢梭菌纤溶酶的纯化及特性  

Purification and Characterization of Fibrinolytic Enzyme of C. SporogenesStrain

作　　者：赵红[1] 程洁[1] 陆俭[1] 孟筱琦[1] 

机构地区：[1]兰州生物制品研究所,兰州730046

出　　处：《中国生物制品学杂志》2002年第1期27-31,共5页Chinese Journal of Biologicals

摘　　要：目的 从产芽孢梭菌的培养上清中分离纯化出具有纤溶活性的蛋白质。方法 以产芽孢梭菌的培养上清为材料，经过滤、硫酸铵盐析、离子交换层析纯化纤溶酶，并对其理化特性和纤溶活性进行鉴定。结果 所分离纯化的纤溶酶相对分子质量为67000，系由相对分子质量45000和20000的2个亚基组成，具有较强的溶解纤维蛋白的作用。此酶属丝氨酸蛋白酶类，胰蛋白酶类。结论 为纤溶酶的开发和应用提供了依据。Abstract : Objective To purify the protease with fibrinolytic activity from the culture supernatant of Clostridium sporogenes . Methods Fibrinolytic enzyme was purified from the culture supernatant of Clostridi-um Sporogenes by filtration, precipitation with ammonium sulfate and ion - exchange chromatcgraphy, and the physicochemical property and fibrinolytic activity of it were characterized. Results The purified fibrinolytic enzyme, with a relative molecular weight of 67000, consisted of two subunits with the relative molecular weights of 45000 and 20000 respectively. It showed strong fibrinolytic activity. The enzyme was a kind of serine protease with trypsin - like activity. Conclusion The study provides a reliable basis for the development and application of fibrinolytic enzyme.

关 键 词：产芽孢梭菌 纤溶酶 纯化 管理 

分 类 号：Q936[生物学—微生物学] TQ925[轻工技术与工程—发酵工程]