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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 HIVgp41 in E. coli. Methods The envelope protein env gene (gp4 1) of HIV 1SF2 strain was purified by PCR and cloned into prokaryotic expression vector pBV220 and expressed in E. coli HB10 1. Results SDS PAGE electrophoresis showed that there was a protein expression band at 4400. Western blot showed that the 4 0 0 0 protein band can specifically react with HIV 1-positive serum. Conclusion The recombinant fusion protein gp4 1 can be HIV 1 gp4 1.