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。
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.
出处
《中国生物制品学杂志》
CAS
CSCD
2000年第1期27-29,共3页
Chinese Journal of Biologicals
关键词
乙型肝炎病毒
x-蛋白
包涵体
亲和层析
Hepatitis B virus x-protein Inclusion body Affinity chromatography