猪型布鲁氏菌omp31基因的原核表达与亲和纯化

Sequence cloning and prokaryotic expression of omp31 gene in swine Brucella

以猪型布鲁氏菌基因组作为模板进行基因序列的扩增,利用大肠杆菌原核表达系统进行重组表达,来研究外膜蛋白基因omp31的序列特性与重组表达情况。结果表明:猪型布鲁氏菌omp31基因的开放阅读框序列全长为723 bp,编码240个氨基酸。通过大肠杆菌原核表达,成功表达出了目标重组蛋白,利用GSTtag亲和柱进行蛋白质纯化,重组蛋白分子量与预期的55.3 kD相一致。

In this paper , the swine Brucella genome was used as the template to amplify the omp31 gene sequence and its sequence characteristics and recombinant expression through E.coli prokaryotic expression system were also invetigated.The results showed the ORF sequence of omp31 gene included 723 bp, and it encoded 240 amino acids. The recombinant protein Omp31 was successfully expressed by E.coli prokaryotic expression system .The recombi-nant protein was purified by GST-tag affinity column , and the molucelar was consistent with the expected 55.3 KD.