蚯蚓纤溶酶的分离及其生物学特性  

Study on separation purification and characterization of the fibrinolysin from earthworms

作　　者：李长公 曾耀辉[1] 

机构地区：[1]清华大学生物科学与技术系

出　　处：《清华大学学报（自然科学版）》1993年第3期100-106,共7页Journal of Tsinghua University(Science and Technology)

摘　　要：经过分离纯化，从人工养殖的赤子爱胜蚓中提取出两种既有纤维蛋白溶酶原激活因子活性又能直接溶解纤维蛋白的组分。ＰＡＧＥ检测各为一条区带，证明已达电泳纯。对这两组分的生物学性质进行了研究，包括分子量、酶活力，Ｎ－末端氨基酸残基，氨基酸组成，温度的稳定性及对苯甲酸精氨酸乙酯（ＢＡＥＥ）的酶促反应动力学特性。还分析了其中一个组分（ＢⅡ）从Ｎ末端开始的 ２５个氨基酸残基序列。Two proteases with the activity of fibrinolysin were purified from earthworms. The PAGE pattern showed that each of the purified products was single component material. The properties and composition of the proteases were determined, including: a) molecular woight, b)enzyme activity, c) N-ternimal amino acid, d) amino acid composition, e) stability at certain temperature, f) the Km values of the proteases toward BAEE.

关 键 词：蚓蚯 蛋白酶 纤溶酶 分离 

分 类 号：Q55[生物学—生物化学]