摘要
本文将免疫筛选的阳性克隆转染大肠杆菌Y_(1039),IPTG诱导,表达产物经SDS-PAGE后银染色,显示有一条大于β-半乳糖苷酶(Mw=116kDa)的融合蛋白条带,分子量约140—150kDa.融合蛋白能被感染兔血清所识别,ELISA显示抗体滴度为1:1230.结果表明,经免疫筛选的阳性克隆能在大肠杆菌中诱导表达,表达产物为日本血吸虫抗原.
The positive colnes obtained by immunoscreening were introduced as lysogens into the E. coli host strain Y1089-and induced by IPTG. The expressed products all showed a band of fusion protein with E. coli β-galactosidase with SDS-PAGE followed by silver staining. The molecular weight of fusion proteins was about 140-150kDa which was larger than β-galactosidase (Mw = 116kDa). The fusion proteins could be recognized by IRS. The dilution of antibody was 1 :1280. The results indicated that the positive clones obtained by immunoscreening could be expressed in E. coli and the expression products were Schistosoma japonicum antigens.
出处
《咸宁医学院学报》
1996年第1期1-3,共3页
Journal of Xianning Medical College
