摘要
利用PCR和基因重组技术构建了小鼠PC-1基因全长cDNA及其N端45个氨基酸残基的表达质粒pGEX-4T-1-mPC-1和pGEX-4T-1-mPC-1-45。经IPTG诱导后,在大肠杆菌DH5α中,GST-mPC-1和GST-mPC-1-45两个融合蛋白都获得了可溶性高表达。经谷胱甘肽Sepharose-4B亲和柱层析纯化后,获得了纯的GST-mPC-1和GST-mPC-1-45蛋白。
Utilizing PCR and gene recombination technologies,two expression plasmids,pGEX-4T-1-mPC-1and pGEX-4T-1-mPC-1-45,were constructed,which contains the entire murine PC-1gene cDNA and its N-terminus45amino acids,respectively.Induced by IPTG,two fusion proteins,GST-mPC-1and GST-mPC-1-45,were ex-pressed soluble in E.coli strain DH5α.Purified proteins,GST-mPC-1and GST-mPC-1-45,were obtained after Glu-tathione Sepharose-4B chromatography.
出处
《生物技术通讯》
CAS
2002年第6期424-426,429,共4页
Letters in Biotechnology
基金
国家自然科学基金(30070296)
