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Expression and Purification of ZNF191(243-368) in Three Expression Systems
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作者 赵东欣 滕欣辰 +1 位作者 丁志春 黄仲贤 《Chinese Journal of Chemistry》 SCIE CAS CSCD 2007年第11期1739-1742,共4页
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, thre... 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. 展开更多
关键词 protein expression affinity chromatography fusion protein isopropylthio-β-d-galactoside
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