摘要
为构建抗结核病新型疫苗 ,以结核杆菌标准毒力株H37RvDNA为模板 ,用PCR法克隆抗原 85B的编码基因 .将该基因重组到表达型质粒pQE30中 ,表达的His6Tag Ag85B融合蛋白分子质量约 32ku .用亲和层析一步法纯化的重组蛋白纯度好、得率高 。
Using virulent strain of Mycobacterium tuberculosis,H37Rv, as template, the coding sequence of mature Ag85B was cloned in pQE30 by PCR. The recombinant protein from the extracts of stable transfected TG1 was purified by one step affinity chromatography. The molecular mass of the product, with RGS His6 tag, is 32 ku. The purity and quantity of the purified recombinant protein is satisfactory, which will assist further research work on Ag85B.
出处
《复旦学报（自然科学版）》
CAS
CSCD
北大核心
2002年第1期113-116,共4页
Journal of Fudan University：Natural Science
关键词
结核杆菌
抗原85B
基因表达
mycobacterium tuberculosis
Ag85B
gene expression
