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用疏水色谱法纯化基因重组 牛朊病毒正常成熟蛋白
引用本文:耿信笃,王超展,张养军,申烨华,王大伟,田波.用疏水色谱法纯化基因重组 牛朊病毒正常成熟蛋白[J].纺织高校基础科学学报,2001,14(1):1-5,33.
作者姓名:耿信笃  王超展  张养军  申烨华  王大伟  田波
作者单位:1. 西北大学 现代分离科学研究所,
2. 中国科学院微生物研究所 分子病毒学与生物工程研究室,
基金项目:国家自然科学基金资助课题(29675017,3988003)
摘    要:研究并比较了高效疏水相互作用色谱(HPHIC)的流动相组成、固定相、pH值和梯度方式对分离基因重组大肠杆菌高效表达的牛朊病毒正常成熟蛋白的影响,在此基础上,确定了牛朊病毒正常成熟蛋白分离纯化的最优化条件,即仅用高效疏水色谱法坦 步便可得到纯度和质量回收率均大于90%的目标蛋白,还讨论了用HPHIC对变性bPrP^cL的分离机理。

关 键 词:  朊病毒  高效疏水色谱  蛋白分离纯化  基因工程
文章编号:1006-8341(2001)01-0001-05

The purification of recombinant bovine mature PrPc by high performance hydrophobic lnteraction chromatography
GENG Xin-du.The purification of recombinant bovine mature PrPc by high performance hydrophobic lnteraction chromatography[J].Basic Sciences Journal of Textile Universities,2001,14(1):1-5,33.
Authors:GENG Xin-du
Abstract:The effects of composition of mobile phase,stationary phase,pH and gradient mode for high performance hydrophobic interaction chromatography(HPHIC) on the separation of recombinant bovine mature PrP c highly expressed in E.Coli were studied and compared.An optimum condition for the separation and purification of recombinant bovine mature PrP c by HPHIC was reported.Both the purity and the mass recovery of bPrP cL were more than 90% only by one step HPHIC.In addition,the separation mechanism of unfolding bPrP cL by HPHIC was also discussed.
Keywords:PrP  c  high performance hydrophobic interaction chromatography  separation and purification of protein  biotechnology
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