论文部分内容阅读
将我国恶性疟原虫ＦＣＣ－１／ＨＮ株ＭＳＡ１第二区基因（ＭＳＡ１Ｒ２）和ＭＳＡ２全基因克隆入ｐＷＲ４５０－Ｉ表达载体中，在大肠杆菌中表达了ＭＳＡ１Ｒ２和ＭＳＡ２与β－半乳糖苷酶的融合蛋白，分子量分别为７２ｋＤ和９４ｋＤ，约占菌体蛋白总量的２５—３０％和５—８％。用兔抗恶性疟原虫血清进行Ｗｅｓｔｅｒｎｂｌｏｔ分析，诱导的ｐＷＲ－ＭＳＡ１Ｒ２和ｐＷＲ－ＭＳＡ２工程菌分别在７２ｋＤ和９４ｋＤ处出现与抗恶性疟抗体反应的特异染色区带，而未经诱导的工程菌和ｐＷＲ４５０Ｉ转化菌则无反应。对ＭＳＡ２－ｐＷＲ工程菌在诱导后出现的工程菌生长缓慢、表达量低、表达产物分子量偏大等异常现象进行了分析。
The whole gene of MSA1 gene MSA1 and MSA2 of Plasmodium falciparum FCC-1 / HN strain was cloned into pWR450-I expression vector and the fusion of MSA1R2 and MSA2 with β-galactosidase was expressed in Escherichia coli Proteins with molecular weights of 72 kD and 94 kD respectively, accounting for 25-30% and 5-8% of the total bacterial proteins. Western blot analysis of rabbit anti-Plasmodium falciparum serum revealed that the induced specific bands of pWR-MSA1R2 and pWR-MSA2 at 72 kD and 94 kD, respectively, reacted with the anti-Plasmodium falciparum antibody, whereas the un-induced engineering bacteria and pWR450I Transformation of bacteria is no reaction. After the induction of MSA2-pWR engineered bacteria engineering bacteria showed slow growth, low expression, the expression of molecular weight is too large and other anomalies were analyzed.