中文摘要：

将丁香假单胞菌番茄变种DC3000（P.syringae pv.tomato DC3000）极毛蛋白hrpA基因克隆到pET32a（＋）载体上,获得重组表达载体pET32a（＋）-hrpA.将重组质粒转入宿主E.coli BL21（DE3）溶源菌中,通过SDS-PAGE分析表明,在1.0mmol.L-1异丙基硫代-β-D半乳糖苷（IPTG）的诱导下,重组子成功表达了分子质量约为28 ku的融合蛋白（目标蛋白基因与硫氧还蛋白基因的融合表达产物）.并利用Ni2＋-NTA柱亲和层析分离获得纯化的HrpA蛋白,质量浓度为91.8 g.L-1.

英文摘要：

HrpA gene was obtained from Pseudomonas syringae pv.tomato DC3000 by PCR and the protein expression system of Escherichia coli BL21（DE3） for hrpA was constructed with vector pET32a（＋）.SDS-PAGE analysis showed that the transformant with recombinant expression plasmid pET32a（＋）-hrpA produced a fusion protein of TrxA-HrpA with corresponding molecular weight of 28 ku.Furthermore,HrpA recombination protein was purified through Ni2＋-NTA and its concentration was measured to be 91.8 g·L-1.