摘要
目的:获得大量重组MgrA蛋白,为深入研究其功能提供必要的材料。方法:用构建好的含有目的基因mgrA的His融合表达载体,转化大肠杆菌感受态细胞,在IPTG诱导下进行高密度发酵,对所得蛋白进行纯化、复性,以SDS-PAGE凝胶电泳检测鉴定其特性。结果:①表达诱导菌体的裂解上清经金属螫合亲和层析,聚丙烯酰胺凝胶电泳证实获得初步纯化的蛋白中仍含一些杂蛋白。②重组获得多个蛋白洗脱峰,再经聚丙烯酰胺凝胶电泳法证实获得纯度较高的目的蛋白。结论:获得了纯化的MgrA蛋白重组蛋白。
Objective:To obtain generous recombined MgrA protein and provide essential data for lucubrating its function.Methods:Colibacillus competent cells were transformed by His fusion expression vector that contained target gene,and then proceeded high density fermentation induced by IPTG.The protein purified and renaturated,and evaluated by SDS-PAGE gel electrophoresis.Results:①The initially purified protein was verified by SDS-PAGE gel electrophoresis,but also contained some hybridprotein.②Multiple protein eluting peak were obtained and high purity taget protein was verified by SDS-PAGE gel electrophoresis.Conelusions: We obtain purified recombined MgrA protein.
出处
《承德医学院学报》
2009年第1期14-16,共3页
Journal of Chengde Medical University
