2010•Shanghai nongye xuebaoRequires access
Optimization of expression conditions of PRRSV GP5 and N proteins in E.coli and purification of expression products
Chunling Zhang, Wanhua Zhang, Chunhua Li, Fengying Jiang, Zhou ZongQing, HE Xi-zhong, Zhu YongJun, Su WanGuo, Yong Zou
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Abstract
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℃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.