摘要
目的 探讨基因工程菌PEB1 E.coli BL21（DE3）大量表达重组空肠弯曲菌PEB1蛋白的稳定性及其纯化方法并鉴定.方法 诱导培养工程菌E.coli BL21（DE3）表达重组空肠弯曲菌PEB1蛋白,经镍琼脂糖凝胶层析柱纯化,透析后通过SDS-PAGE分析纯化后的重组空肠弯曲菌PEB1蛋白分子量大小.结果 挑取的PEB1 E.coli BL21（DE3）单个菌落,经总共17 h的扩增,细菌总数可达1×1010以上.在咪唑浓度为100,200,300 mmol/L时,洗脱液中重组蛋白的含量较高,分子量在31KD左右.结论 基因工程菌PEB1 E.coli BL21（DE3）可大量稳定表达重组空肠弯曲菌PEB1蛋白,经鉴定与空肠弯曲菌外膜蛋白-PEB1蛋白分子量相同.
Objective To express recombinant PEB1 protein of CJ and prepare,identify the recombinant PEB1 protein of CJ. Methods E. coli BL21 （DE3） was raised and induced to express the recombinant CJ PEB1 protein. Then the recombinant protein was purified by the nickel agarose column,dialyzed in the dialysis bag and quantitated by BCA kit. Results The recombinant PEB1 protein with high purity was obtained whose molecular weight was identical with theory value. Conclusion The E. coli BL21（DE3） could express CJ PEB1 protein stably, which was identical with theory value.
出处
《现代检验医学杂志》
CAS
2011年第5期41-43,共3页
Journal of Modern Laboratory Medicine
基金
贵州省优秀人才省长基金课题（黔科教办[2006]07）资助.
关键词
重组
空肠弯曲菌
PEB1蛋白
表达
鉴定
recombinant
Campylobacter jejuni
PEB1 protein
expession
identification
