抑肽酶的提取及活性研究  

Isolation of Aprotinin and Study on Its Inhibition Activities

作　　者：赵清海[1] 王霞红[1] 陈树瑛 陆国芳 张天仁[1] 

机构地区：[1]卫生部上海生物制品研究所,上海200052

出　　处：《中国生物制品学杂志》1992年第3期108-110,共3页Chinese Journal of Biologicals

摘　　要：以牛肺为原料,经酸沉淀,胰蛋白酶亲和层析,分离提纯抑肽酶。并建立了二种抑肽酶活性测定方法(UKIU法及PKAIU法)。提纯后抑肽酶纯度提高88.3倍。得率为96.8％。活性抑制试验表明,该抑肽酶可抑制PKA对前激肽释放酶(PK)的作用,以及尿激酶对纤溶酶原的作用,对纤溶酶原的活化及纤溶酶活性也有较强抑制作用。Aprotinin was isolated from bovin lung by means of homogenizing, TCA precipitation and trypsin Sepharose 4B affinity ehrornatography. The methods of assaying the UK inhibition unit(UK/U) and PKA inhibition unit (PKAIU) were established for testing aprotinin activities. The specific activity of purified aprotinin increased by 88.3 folds and recovery was 96.8%. Results of inhibition tests showed that the aprotinin inhibited PKA as well as UK activities. The aprotinin also prolonged the fibrinolysis time of fibrin gel from 36 to 144h. Thus, it suggested that plasmin could be strongly inhibited by the aprotinin.

关 键 词：抑肽酶 纤维蛋白凝胶 纤维蛋白粘合剂 纤溶酶 尿激酶 激肽释放酶 

分 类 号：R977[医药卫生—药品]