摘要
采用自制的酰基化－Ｐｌｇ－Ｓｅｐｈａｒｏｓｅ４Ｂ亲和层析分离纯化链激酶，ＮＰＧＢ作为酰化剂，８ｍｏｌ／Ｌ尿素进行洗脱，纯化约９倍，收率９０％以上，比活为７４０００Ｕ／ｍｇ蛋白质，ＳＤＳ－ＰＡＧＥ显示链激酶分子量为４７０００，未发生降解。ＮＰＧＢ酰化稳定，一次酰化后可反复使用２０余次。
Streptokinase (SK) was purified by affinity chromatography on immobilized pnitrophenyl pguanidinobenzoate (NPGB) acylated plasminogenSepharose 4B.Urea (8 mol/L) was used as an eluent.The specific activity of SK reached 74000 U/mgpro with approximate 9fold of purification and over 90% yield.SDSPAGE showed a predominant band of 47kd,corresponding to the standard SK sample.After acylation of NPGB,the gels were quite stable,and have been used over twenty times.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
1999年第6期241-242,共2页
Chinese Journal of Pharmaceuticals
关键词
链激酶
分离
纯化
亲和层析
streptokinase,purification,affinity chromatography
