牙鲆Myogenin蛋白在大肠杆菌中重组表达的研究  

Recombinant Expression of Flounder Myogenin in Escherichia coli

作　　者：徐芃[1] 谭训刚[1] 张培军[1] 王先磊[1] 张玉青[1] 

机构地区：[1]中国科学院海洋研究所实验海洋生物学重点实验室

出　　处：《中国海洋大学学报（自然科学版）》2007年第5期754-758,共5页Periodical of Ocean University of China

基　　金：国家重点基础研究发展规划项目(2004CB117402);国家高技术研究发展计划项目(20060110A4013)资助

摘　　要：采用大肠杆菌表达系统及pProEXTMHTc表达载体对牙鲆肌肉发生调节因子myogenin基因进行了体外重组表达研究。通过对诱导时间、IPTG诱导浓度以及诱导温度的优化,确定了最佳诱导条件为:诱导温度31℃,IPTG终浓度0.6mmol/L,诱导时间2 h。在该条件下,重组蛋白表达量最高且是可溶性的。Myogenin融合蛋白的成功表达为进一步深入研究其在牙鲆肌肉发育过程中的分子机制奠定了基础。The flounder myogenin was cloned, ligated into prokaryotic expression vector pProEX^TMHTc and expressed in strain E. coli BL21 （DE3）. To optimize induced conditions and obtain the soluble recombinant protein, the effects of different induction times, IPTG concentrations and temperatures on the expression of Myogenin recombinant protein were analyzed. SDS-PAGE analysis showed that the protein could be expressed at high levels when it was induced by 0.6 mmol/L IPTG for 2 h at 31 ℃. And the recombinant protein was proved to be soluble under these induction conditions. Myogenin recombinant protein will be useful for further studies on the mechanism of flounder myogenesis.

关 键 词：牙鲆 体外蛋白表达 MYOGENIN 

分 类 号：Q78[生物学—分子生物学]