文献类型：期刊文献

中文题名：重组大肠杆菌Trx-hPTH蛋白在双水相体系内的初步纯化

英文题名：Partial Purification of Human Parathyroid Hormone 1-84 as a Thioredoxin Fusion Form Expressed by Recombinant Escherichia coli in Aqueous Two-Phase System

作者：刘珊珊[1];王风清[1]

机构：[1]华东理工大学生物反应器工程国家重点实验室,上海200237

年份：2009

卷号：35

期号：1

起止页码：35

中文期刊名：华东理工大学学报（自然科学版）

外文期刊名：Journal of East China University of Science and Technology

收录：CSTPCD;;Scopus;北大核心:【北大核心2008】；CSCD:【CSCD2011_2012】；

语种：中文

中文关键词：双水相;Trx-hPTH蛋白;纯化;大肠杆菌

外文关键词：aqueous two-phase system; human parathyroid hormone 1-84; purification; Escherichia coli;

摘要：用双水相体系萃取技术对重组大肠杆菌表达的人甲状旁腺激素融合蛋白Trx-hPTH进行了初步纯化,考察了盐的种类、PEG的平均分子量及浓度、MgSO4浓度、pH等因素对Trx-hPTH蛋白在PEG-MgSO4体系内分配行为的影响。结果表明:当双水相体系中w(MgSO4)=0.16,w(PEG 1000)=0.20,pH为8.0时,一步萃取后目标蛋白的分配系数为3.4,回收率为88.6%。
The partitioning of Trx-hPTH（1-84） （human parathyroid hormone coupled with thioredoxin as a fusion partner） expressed by recombinant E. coli in the aqueous two-phase system（ATPS） comprised of PEG and salts was investigated. The effective factors on partition including the molecular weight and concentration of PEG, the types and concentration of salts and pH were evaluated. The maximum partitioning of the protein （K=3.4,Y=88. 6%） was achieved in the ATPS when w（PEG 1000）=0.20 and w（MgSO4） =0. 16 with the protein in the top PEG rich phase.