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作 者:Yicun Wang Feng Zhang Haiwei Chen Xiwen Chen Defu Chen
机构地区:[1]Laboratory of Molecular Genetics,College of Life Sciences,Nankai University [2]College of Life Sciences,Chifeng College,Chifeng 024000,China
出 处:《Journal of Genetics and Genomics》2013年第6期319-322,共4页遗传学报(英文版)
基 金:supported by the grants of the National Natural Science Foundation of China(No.31070717);Tianjin International Science and Technology Cooperation Project (No.09ZCGHHZ00500);the 111 Project(No.B08011)
摘 要:Expression of recombinant protein in Escherichia coli (E.coli) is generally considered as one of the ideal systems to produce proteins for industrial production.However,the majority of proteins usually fail to fold into their native state and accumulate as insoluble inclusion bodies with no biological activity in E.coli(Yang et al.,2003).Expression of recombinant protein in Escherichia coli (E.coli) is generally considered as one of the ideal systems to produce proteins for industrial production.However,the majority of proteins usually fail to fold into their native state and accumulate as insoluble inclusion bodies with no biological activity in E.coli(Yang et al.,2003).
关 键 词:Directed Evolution of Insoluble Arabidopsis thaliana Zeta Class Glutathione S-Transferase Mutants for Higher Solubility in Escherichia coli coli
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