摘要
本文对两个重组人γ干扰素高表达菌株pIFN-γ及pBV871的表达产物进行了纯化,用盐酸胍裂解菌体,硫酸铵沉淀法去除杂蛋白,酸沉淀法浓缩干扰素,然后经单克隆抗体亲和层析柱纯化,可纯化945倍,达电泳纯级,回收率达30％,比活性达7.56×10~7U/mg蛋白,SDS-PAGE电泳上γ干扰素分子量约17500d。
Recombinant human interferon gamma produced in E.coli carrying pIFN-γ or pBV871 was purifid to homogeneity with a recovery of 25-30%, using a series of successive purification steps. The purified rHuIFN showed a single band of MWW 17500 dalton on SDS-PAGE. The specific activity of the purified rHuIFN-γ reached more than 5×107U/mg protein.
出处
《病毒学报》
CAS
CSCD
北大核心
1989年第1期37-40,共4页
Chinese Journal of Virology
