| 大肠杆菌表达的rhGM—CSF发酵纯化工艺研究 |
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| 引用本文： | 段淑敏,李福胜,杨新科,陈文涛. 大肠杆菌表达的rhGM—CSF发酵纯化工艺研究[J]. 中国生物制品学杂志, 1996, 9(3): 124-128 |
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| 作者姓名： | 段淑敏 李福胜 杨新科 陈文涛 |
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| 作者单位： | 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(段淑敏，李福胜，杨新科)，深圳新鹏生物制品公司(陈文涛) |
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| 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。
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| 关 键 词： | 重组人粒细胞-巨噬细胞集落刺激因子 大肠杆菌 |
Study on Fermentation and Purification Process for rhGM-CSF Expressed in E.coli |
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| Duan Shumin, Li Fusheng, Yang Xinke ct al. Study on Fermentation and Purification Process for rhGM-CSF Expressed in E.coli[J]. Chinese Journal of Bilogicals, 1996, 9(3): 124-128 |
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| Authors: | Duan Shumin Li Fusheng Yang Xinke ct al |
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| Abstract: | 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. |
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| Keywords: | rhGM-CSF-Fermentation-Purification |
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