Expression and Purification of ZNF191（243-368） in Three Expression Systems  

作　　者：赵东欣 滕欣辰 丁志春 黄仲贤 

机构地区：[1]Department of Chemistry, Fudan University, Shanghai 200433, China [2]School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou, Henan 450001, China

出　　处：《Chinese Journal of Chemistry》2007年第11期1739-1742,共4页中国化学（英文版）

基　　金：Project supported by the National Natural Science Foundation of China （Nos. 30170228, 39990600）.Acknowledgements We thank Prof. Long Yu （Fudan University） for the ZNF191 gene.

摘　　要：ZNF191 （243-368）, a new human zinc finger protein, probably relates to some hereditary diseases and cancers, To obtain adequate amount of ZNF191（243-368） for the study of its property, structure and function, three different expression systems of inclusion-body, glutathione S-transferase （GST）, and hexahistidine （6 × His） were used and compared. Among these systems, the expression level of ZNFI91（243-368） was increased in inclusion body system under a higher isopropylthio-β-D-galactoside （IPTG） concentration, but the non-target proteins were also increased more, which made its purification more difficult and the yield lower. The expression of His-tag fusion protein was almost not affected by IPTG concentration, temperature and inducing time. At a high IPTG concentration the highest expression yield for GST fusion protein was obtained. And the fusion proteins can be partially purified by a single affinity chromatography step. The fusion protein systems show advantages for expression of these proteins.ZNF191 （243-368）, a new human zinc finger protein, probably relates to some hereditary diseases and cancers, To obtain adequate amount of ZNF191（243-368） for the study of its property, structure and function, three different expression systems of inclusion-body, glutathione S-transferase （GST）, and hexahistidine （6 × His） were used and compared. Among these systems, the expression level of ZNFI91（243-368） was increased in inclusion body system under a higher isopropylthio-β-D-galactoside （IPTG） concentration, but the non-target proteins were also increased more, which made its purification more difficult and the yield lower. The expression of His-tag fusion protein was almost not affected by IPTG concentration, temperature and inducing time. At a high IPTG concentration the highest expression yield for GST fusion protein was obtained. And the fusion proteins can be partially purified by a single affinity chromatography step. The fusion protein systems show advantages for expression of these proteins.

关 键 词：protein expression affinity chromatography fusion protein isopropylthio-β-D-galactoside 

分 类 号：O62[理学—有机化学]