首页 | 本学科首页   官方微博 | 高级检索  
     

从包涵体中高效纯化HBx-蛋白
引用本文:颜华,方志正.从包涵体中高效纯化HBx-蛋白[J].粉末涂料与涂装,2000,13(1):27-29.
作者姓名:颜华  方志正
作者单位:[1]武汉生物制品研究所,武汉 [2]德国国家肿瘤研究所,武汉
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。

关 键 词:乙型肝炎病毒  x-蛋白  包涵体  亲和层析

High Purification of HBx-protein from Inclusion Body
Clarus H.Schroeder,Yan Hua,Fang Zhizheng,Clarus H.Schroeder.High Purification of HBx-protein from Inclusion Body[J].Chinese Journal of Biologicals,2000,13(1):27-29.
Authors:Clarus HSchroeder  Yan Hua  Fang Zhizheng  Clarus HSchroeder
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.
Keywords:Hepatitis B virus x-protein Inclusion body  Affinity chromatography
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号