大肠杆菌表达的rhGM—CSF发酵纯化工艺研究  

Study on Fermentation and Purification Process for rhGM-CSF Expressed in E.coli

作　　者：段淑敏[1] 李福胜[1] 杨新科[1] 陈文涛 

机构地区：[1]中国预防医学科学院病毒基因工程国家重点实验室,北京100052 [2]深圳新鹏生物制品公司

出　　处：《中国生物制品学杂志》1996年第3期124-128,共5页Chinese Journal of Biologicals

摘　　要：重组人粒细胞-巨噬细胞集落刺激因子（rhGM－CSF）基因表达产物在大肠杆菌的胞浆中以不溶性包涵体的形式存在、包涵体用超声破菌分离后，经变性、复性，用流水层析、离子交换层析、凝胶过滤层析等进行纯化。SDS—PAGE表明终产物纯度达97．8％。纯化蛋白的比活性根据MTT法在TF—1细胞测定的结果，可达3×107u／mg蛋白。The recombinant human granulocyte-magrophage colony stimulating factor (rhGM -CSF) expressed in E, coli exists in the form of insoluble inclusion bodies. The inclu-sion bodies were separated from cytoplasm by ultrasonication. After denaturation and renatu-ration, they were purified by hydrophobic, ion exchange and gel filtration chromatographies.From SDS-PAGE pattern, the purity of final product reached 97. 8 %,and the specific activi-ty detected by MTT method using TF-1 cell reached 3×107 u/mg protein.

关 键 词：粒细胞巨噬细胞 集落刺激因子 RHGM-CSF 发酵 

分 类 号：R392－33[医药卫生—免疫学] TQ929[医药卫生—基础医学]