摘要
采用不同的培养基、诱导温度、诱导时间、IPTG诱导剂浓度以及诱导菌浓度等大肠杆菌表达条件,进行了融合蛋白HIS-GP5和HIS-N的优化表达和纯化研究。结果表明:重组质粒转化菌E.coli BL21(DE3)在含0.3mmol/L IPTG的TB培养基中,20℃诱导表达14 h时融合蛋白表达量最高,经纯化得到了HIS-GP5和HIS-N融合蛋白。SDS-PAGE电泳分析表明,纯化的蛋白纯度大于95%。
The optimization expression and purification of HIS-GP5 and HIS-N fusion proteins were studied by changing such E. coli expression conditions as culture medium,induction temperature and time, and IPTG inducer concentration. The results showed that the expressed fusion proteins reached the maximum when induced in TB culture medium containing 0.3 mmol/L IPTG at 20 ~C for 14 h,and the HIS-GP5 and HIS-N fusion proteins were obtained through purification. The SDS-PAGE electrophoretic analysis indicated that the soluble proteins after further purification were over 95 % in purity.
出处
《上海农业学报》
CSCD
北大核心
2010年第3期17-20,共4页
Acta Agriculturae Shanghai
基金
上海市科委重点攻关计划(053919117)资助
