乙型肝炎病毒表面抗原(HBsAg)的高效表达和分离纯化  

The Expression and Purification of HBV Surface Protein(HBsAg)

作　　者：周世力[1] 韩雪[1] 郜金荣[2] 叶林柏[2] 吴正辉[2] 

机构地区：[1]江汉大学医学与生命科学学院,武汉430056 [2]武汉大学生命科学学院

出　　处：《分析科学学报》2007年第3期269-272,共4页Journal of Analytical Science

摘　　要：从病人血清中采用PCR扩增得到了编码HBV-HBsAg蛋白的S基因片段,将其转入PET-His表达载体,构建了原核表达质粒pET-His-HBsAg,转化大肠杆菌BL21,IPTG诱导表达。收获菌体超声波破碎后,梯度蔗糖溶液洗脱杂质。HBsAg在原核系统中高效表达分子量为25 kDa,并得到了纯度为97%的HBsAg蛋白。为进一步研究HBsAg奠定了基础。We extracted Hepatitis B virus （HBV） S DNA from HBV patient human serum, and constructed recombinant plasmids pET-his-HBsAg which was transformed into BL21 and induced with IPTG. The HBsAg protein was pufifed by the sucrose density gradient centrifugation. The HBsAg protein was expressed efficiently in the E. coli with the molecular wieght of 25 kDa and the purity was 97% The highly efficeint expression and purification of HBsAg protein laid a foundation for further HBsAg reseaching.

关 键 词：HBV-HBsAg 表达 分离纯化 

分 类 号：Q934.2[生物学—微生物学]