【摘要】 目的　从大肠杆菌中获得载脂蛋白A I(米兰变体 ) 的包涵体 ,对包涵体进行复性、纯化 ,最终获得具有生物活性的载脂蛋白A I(米兰变体 ) 。方法　包涵体以尿素溶解后 ,以疏水层析法复性重组蛋白 ;以离子交换层析对其进一步纯化 ,并对所得的蛋白进行生物活性分析。结果　经复性纯化的蛋白纯度达 95 % ,体外生物活性检测显示其具有生物活性。结论　本法能快速有效地对目的蛋白进行复性、纯化 ,并且有望放大至工业生产规模更多还原

【Abstract】 Objective To express the inclusion body containing Apo A I M in E.coli ,then renaturalize and purify to obtain biologically active Apo A I M.Methods Dissolve inclusion body with urea and renaturalize the recombinant protein by hydrophobic chromatography,then further purify by ion exchange chromatography.The obtained protein was subject to bioassay.Results The purity of recombinant protein after renaturation and purification reached 95%.The protein was proved to be biologically active by in vitro bioassay.Conclusion The method was suitable for the rapid and effective renaturation and purification of goal protein,so it is hopeful to be applied in industrial scale production.更多还原