摘要
目的 研究人乳头状瘤病毒(HPV)主要结构蛋白L1(HPV16L1)和次要结构蛋白L2(HPV16L2)在原核系统的表达。方法 采用pET30a载体分别构建pET30aL1和pET30aL2质粒,并分别转入大肠埃希菌BL21菌株,经IPTG(异丙基硫代βD半乳糖苷)诱导,表达融合蛋白6×HisL1和6×HisL2,用SDSPAGE和Westernblot方法进行检测。结果 6×HisL1和6×HisL2融合蛋白在BL21菌中高效表达,约2～3mgml,其相对分子质量分别约为60000和97000;6×HisL1降解较6×HisL2多。结论 HPV16结构蛋白L1和L2能在原核表达系统高效表达;6×HisL2稳定性高于6×HisL1融合蛋白。
Objective To study the expression of HPV16 capsid proteins L1 and L2 in E.coli. Methods The plasmids pET 30a L1 and pET 30a L2 were constructed from the pET 30a vector, and transducted into the BL21. The fusion proteins 6×His L1 and 6×His L2 were expressed when induced by adding of IPTG. SDS PAGE and Western blot analyses were used to detect the expressed proteins.Results Fusion proteins 6×His L1 and 6×His L2 were expressed efficiently in E. coli, the Mr were about 60 000 and 97 000 respectively, 6×His L1 degraded more than 6×His L2 .Conclusion L1 and L2 proteins were expressed at a high level in prokaryotic expression system, and L2 protein were more stable than L1 protein.
出处
《中华实验和临床病毒学杂志》
CAS
CSCD
1999年第4期358-361,共4页
Chinese Journal of Experimental and Clinical Virology
基金
国家"九五"重点医学科技攻关专题
关键词
乳头状瘤病毒
基因表达
癌
蛋白质
Papillomavirus
human
Gene protein expression
Cancer
