文献类型： 外文期刊

作者： Qu He-zhi ¹ ; Du shan-shan ¹ ; Yang Shuo ¹ ; Huang Lu ¹ ; Zhang Lei ¹ ; Xiao Song ¹ ; Hao Dong-yun ¹ ; Wang Xiao-ping ¹ ;

作者机构： 1.Jilin Unvers, Minist Educ, Key Lab Mol Enzymol & Engn, Changchun 130021, Peoples R China

2.Jilin Acad Agr Sci, Biotechnol Res Ctr, Changchun 130033, Peoples R China

关键词： Extracellular superoxide dismutase;Protein fusion;Heterologous expression;Pichia pastoris

期刊名称：CHEMICAL RESEARCH IN CHINESE UNIVERSITIES （ 影响因子：1.307； 五年影响因子：0.979 ）

ISSN： 1005-9040

年卷期： 2010 年 26 卷 2 期

页码：

收录情况： SCI

摘要： Mammalian cells express two isoforms of Cu- and Zn-containing superoxide dismutases(SODs), CuZn-SOD and extracellular SOD(EC-SOD), involved in the defense system against reactive oxygen species(ROS). The two SODs have structurally homologous centre domain with distinct N- and C-terminuses, resulting in the different characteristics of the structure and function of the two molecules. We generated a hybrid SOD molecule(namely hySOD) via replacing the N- and C-terminuses of hCuZnSOD with the counterparts of hEC-SOD. The hySOD was expressed in host Pichia pastoris and the purified protein was a dimer with a molecular weight of about 34000. A series of activity analyses indicates that the hySOD is similar to hEC-SOD in heat-stability, and has the activity of protecting the host cell against heat shock and oxidative stress. Our results show evidence for the study on the compound activity of multiple SOD molecules, and may be important for understanding the relationship between structure and function of hEC-SOD and hCuZnSOD.