摘要
该研究将禽网状内皮组织增生病毒gp90基因克隆至原核表达载体pET-30a(+),转化至大肠杆菌BL21(DE3)感受态细胞,经IPTG诱导,并通过SDS-PAGE和Western blotting鉴定蛋白表达情况和蛋白表达.结果发现,将gp90基因连接表达载体转化宿主菌后,成功在大肠杆菌以包涵体形式表达.纯化的蛋白纯度超过90%.
Gp90 gene has been cloned into prokaryotic expression vector pET-30a（＋）. The recombinant vector has been transformed into E. coli BL21 （DE3） competent cells, and the gp90 protein been expressed by IPTG inducing. The expression and the expression form have been identified by SDS-PAGE and Western blotting. The target protein has been purified by protein purification mini Kit. The result show that gpgO gene was ligated into pET-30a（＋） and the recombinant plasmid is transformed into host cell. Recombinant gp90 protein is expressed in the recombinant bacteria as inclusion body. The purity of the purified gp90 protein is more than 90%.
出处
《西南师范大学学报（自然科学版）》
CAS
北大核心
2017年第1期66-69,共4页
Journal of Southwest China Normal University(Natural Science Edition)
基金
"十二五"农村领域国家科技计划项目(2012AA101304-5)
西南大学博士基金(含引进人才计划)项目(SWU114018)
中央高校基本科研业务费专项(XDJK2014B029)
