摘要
继从麻风菌基因组 DNA 库中筛选出α1及α2抗原基因克隆后,我们又探讨了α抗原基因克隆在大肠杆菌中高效率表达的条件和高精度提纯的方法。实验表明,pMALc—RI 质粒为重组α蛋白抗原的最佳表达载体;诱导表达高峰为加入诱导剂后4小时;用亲和层析柱法提纯后,200ml 培养液中重组α1及α2蛋白抗原的检测得量分别约为6mg 和10mg,提取纯度为95%。
Recombinant α1 and α2 antigens of M.leprae have been constructed.The re- combinant α antigen was efficiently expressed on E.coli by using pMALc-RI as an espression vector,and purified by amylose resin affinity chromatography.More than 6 mg and 10 mg re- combinant α1 and α2 proteins were obtained from 200 ml liquid culture respectively.
