【摘要】 目的获得具有生物学活性的重组ＨＢｘ－蛋白。方法经ＴＮＦＭＸ缓冲液清洗表达的包涵体，再将 此包涵体变性，复性后，经亲和层析，分步洗脱、收集。结果获得大量高纯度的ＨＢｘ－蛋白，ＨＢｘ－该蛋白的纯度和回 收率分别达到９６％和２８％。结论此方法具有较好的纯化效果，也可应用于其他重组蛋白的制备。更多还原

【Abstract】 Objective To obtain recombinant HBx-protein with biological acitivity. Methods After expressed inclusion bodies were washed with TNFMX buffer, the HBx-protein in them were degenerated and re- naturated, then purified by affinity chromatography. Results Large amounts of highly purified x-protein were obtained .The purity and recovery rate of the protein reached 96% and 28% respectively. Conclusion The method established by the authors showed good purification effect. It can also be used for the preparation of other recombinant proteins.更多还原