摘要
目的 克隆并在大肠杆菌中表达HIVgp4 1。 方法 应用PCR技术 ,纯化HIV 1SF2 株外膜蛋白env基因 (gp4 1) ,并重组入原核高效表达载体 pBV2 2 0 ,在大肠杆菌HB10 1中进行表达。 结果 SDS PAGE电泳结果表明 ,在 4 4 0 0 0处有一条蛋白表达带。Westernblot证明 ,4 4 0 0 0蛋白带可与HIV 1阳性血清发生特异性反应。结论 该重组表达 gp4 1的融合蛋白 ,可为HIV 1gp4 1。
Objective To clone and express HIV gp41 in E.coli. Method The purified env gene derived from HIV SF 2 strain genome by PCR was recombined with pBV220 which served as high efficiency expression vector and expressed gp41 in E.coli HB101 strain. Results There was a dye band equal to 44 000 displayed by SDS PAGE.It was confirmed that the protein of 44 000 can specially react with HIV 1 positive serum by using Western blot. Conclusion The recombinant protein can be regarded as HIV gp41.
出处
《山西医科大学学报》
CAS
2001年第6期481-483,共3页
Journal of Shanxi Medical University
基金
山东省卫生厅基金资助 (96-12 )