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大肠杆菌冷休克蛋白CspC的分离纯化及部分性质测定
引用本文:刘威,李瑶,向烨,王大成.大肠杆菌冷休克蛋白CspC的分离纯化及部分性质测定[J].生物化学与生物物理进展,2002,29(1):105-109.
作者姓名:刘威  李瑶  向烨  王大成
作者单位:中国科学院生物物理研究所,北京,100101
基金项目:国家自然科学基金资助项目(39970158).
摘    要:经Sepharose Q Fast Flow阴离子交换层析和Superdex 30凝胶过滤层析,从大肠杆菌(Escherichia coli)细胞内分离纯化了一种小分子蛋白质,SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)纯度鉴定为单一条带,经质谱分析、N端测序、同源序列比较,确定该蛋白质为大肠杆菌冷休克蛋白CspC.在此基础上,用圆二色光谱测定了其二级结构含量,初步探索了其热稳定性及与单链DNA结合后的构象变化.

关 键 词:冷休克蛋白,CspC    大肠杆菌,纯化
收稿时间:2001/4/19 0:00:00
修稿时间:2001/6/11 0:00:00

Purification and Partial Characterization of The Cold Shock Protein CspC from Escherichia coli
LIU Wei,LI Yiao,XIANG Ye and WANG Da-Cheng.Purification and Partial Characterization of The Cold Shock Protein CspC from Escherichia coli[J].Progress In Biochemistry and Biophysics,2002,29(1):105-109.
Authors:LIU Wei  LI Yiao  XIANG Ye and WANG Da-Cheng
Institution:Institute of Biophysics, The Chinese Academy of Sciences, Beijing 100101, China;Institute of Biophysics, The Chinese Academy of Sciences, Beijing 100101, China;Institute of Biophysics, The Chinese Academy of Sciences, Beijing 100101, China;Institute of Biophysics, The Chinese Academy of Sciences, Beijing 100101, China
Abstract:After two-step chromatography of Sepharose Q Fast Flow and Superdex 30, a small protein with molecular size of 7.2 ku was purified from Escherichia coli. The purity examined by SDS-PAGE showed as a single band. Its molecular mass measured by mass spectrum and the amino acid sequence of N terminal were in consistence with CspC, one of the cold shock proteins, in E.coli. Subsequently, the content of its secondary structure was estimated from the circular dichroism spectra, and moreover, its stability in high temperature and the conformational change after binding with single strand DNA were monitored with a CD spectrophometer.
Keywords:Escherichia coli  cold shock protein  CspC  purification
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