中文摘要：

将耐氟苯尼考大肠杆菌的floR基因部分基因片段插入pGEX-4T-2原核表达载体中,构建以BL21（DE3）Codon Plus为宿主菌的原核表达体系。通过优化诱导条件,确定了floR1基因能在pGEX/BL21（DE3）codon plus中高效表达,且表达的重组蛋白为包涵体形式。对包涵体进行溶解复性后,将复性融合蛋白过GST亲和层析柱得到纯化的GST-FloR1融合蛋白。并以GST-FloR1融合蛋白为抗原免疫小鼠,成功制备出抗GST-FloR1融合蛋白的抗体。抗体的制备为FloR蛋白定位及其对氟苯尼考药物泵出功能抑制的研究奠定了基础。

英文摘要：

For expressing the recombinant GST-FloR1 protein in prokaryote expression system, floR gene was cloned into pGEX-4T-2, and BL21（DE3） codon plus was chose as corresponding expression hosts. The floR1 gene could be successfully expressed in the systems, by optimizing the IPTG induction concentration, incubation temperature and time. The method of triton-urine with sonication lysis of cells was chose to get the relatively good washing effect. After the protein refolding of denaturant inclusion body following dialysis, we got the pure recombinant GSTFloR1 protein by GST affinity columns. A murine anti-FloR antibody was produced by using the recombinant protein of GST-FloR1 as antigen. The antibody lays the foundation for further research on location of FloR protein and inhibition of drug efllux function.