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Expression and Purification of ZNF191(243–368) in Three Expression Systems
Author(s) -
ZHAO DongXin,
TENG XinCheng,
DING ZhiChun,
HUANG ZhongXian
Publication year - 2007
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200790321
Subject(s) - chemistry , lac operon , fusion protein , fusion , affinity chromatography , protein expression , yield (engineering) , function (biology) , inclusion bodies , chromatography , biochemistry , recombinant dna , microbiology and biotechnology , enzyme , gene , linguistics , philosophy , materials science , biology , metallurgy
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 ZNF191(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.