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。
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.
出处
《南昌大学学报（理科版）》
CAS
北大核心
2003年第3期295-298,共4页
Journal of Nanchang University(Natural Science)
