节点文献
兔防御素NP1在大肠杆菌中的表达
THE EXPRESSION AND PURIFICATION OF FUSION PORTEIN GST-NP1 IN E.Coli
【摘要】 通过选用大肠杆菌偏好密码子对兔防御素基因进行改造,人工合成兔防御素基因并构建编码GST-NP1融合基因,从而在大肠杆菌中进行表达。研究表明:表达的蛋白质经过亲和层析洗脱纯化,SDS-PAGE电泳分析,在目的分子量处出现预期条带。灰度扫描分析表明,表达量最高可达细菌总蛋白的34.7%。经切割、复性后的防御素具有溶血活性。
【Abstract】 The codons of rabbit defensin NP1 gene were modified to eliminate the E.Coli rear codons. The coding region of defensin NP1 was cloned into plasmid pGEX-4T-1, and the fusion protein was expressed in E.Coli JM109.Preliminary study showed that after affinity chromatography there are only one protein band on SDS-PAGE gel. The fusion protein was expressed up about34.7% of total bacterial proteins, and exhibited hemolysis activity after digestion by CNBr and renaturation.
【关键词】 兔防御素;
表达;
大肠杆菌;
溶血活性;
【Key words】 rabbit defensin NP1; E. Coli; gene expression; hemolysis activity.;
【Key words】 rabbit defensin NP1; E. Coli; gene expression; hemolysis activity.;
- 【文献出处】 南昌大学学报(理科版) ,Journal of Nanchang University(Natural Science) , 编辑部邮箱 ,2003年03期
- 【分类号】Q784
- 【被引频次】5
- 【下载频次】86