摘要
目的比较两种方法纯化rhIL-31的效果。方法将含pET32a/rhIL-31的重组菌E.coli.BL21(DE3)经IPTG诱导表达,通过超声波破碎,包涵体的提取溶解,分别经G75凝胶层析和镍琼脂糖凝胶FF层析进行蛋白纯化,通过SDS-PAGE对纯化结果进行比较分析。结果镍琼脂糖凝胶FF层析法的杂蛋白去除率高于凝胶层析法,所得蛋白纯度略高。结论比较重组人IL-31蛋白的纯化效果,镍琼脂糖凝胶FF层析的效果比G75凝胶层析的效果好。
Objective To compare the purification effects of rhIL-31 by two methods.Methods pET32a/rhIL-31 in E.coli.BL21 were expressed when induced by IPTG,E.coli cells were broken by ultrasonic,the inclusion bodies were solvated in urea,further purified respectively by sephadexG-75 gel chromatography and Ni-NTA agarose F.F.,and recombinant human IL-31 protein concentration was determined by SDS PAGE.Results The removal rates of foreign protein of rhIL-31 purified by sephadexG-75 gel chromatography were slightly high...
出处
《中外医疗》
2008年第17期15-16,18,共3页
China & Foreign Medical Treatment
基金
贵州省社会发展课题项目资助(NY20063039)
