摘要
采用PCR方法扩增牛结核杆菌mpb-83基因,并将其连接到T3克隆载体,然后克隆到原核表达载体PET-32 a中,构建重组质粒PET-32 a-mpb-83。以重组质粒转化大肠杆菌BL21,用NI柱纯化,最后纯化产物在SDS-PAGE中检测。结果得到约664 bp的目的片段,且MPB-83可在大肠杆菌BL21中高效表达。
The mpb -83 gene of Mycobacterium boris was cloned by PCR method and was linked with the T3 vector. Then they were inserted into the prokaryotic expression vector PET -32a, which was expressed in E. coli BL21. The purification of mpb - 83 was achieved by NI - NTA agarase and the purified product was analyzed by SDS- PAGE. The results showed that about 664 bp fragment was obtained, and the MPB -83 of Mycobacterium bovis was highly expressed in E. coli.
出处
《山东农业科学》
2010年第6期10-12,共3页
Shandong Agricultural Sciences
基金
山东省中青年科学家基金(BS2009NY002)
山东省农业重大应用技术创新课题(2009)
现代农业产业技术体系(nycytx-0107)资助
