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重组粒单系集落刺激因子（ｒＧＭ－ＣＳＦ）在大肠杆菌中以包涵体形式表达。在实验室规模分离纯化的基础上，我们进行了中试分离纯化研究，优化了发酵、破菌、包涵体的回收、产物的抽提、复性、色谱分离及放大过程。根据包涵体表达产物的共性，第一步分离用分子排阻层析可以除去大部分大分子杂质，进一步的纯化方案根据包涵体溶解试剂和产物本身的分子特性采用阴离子交换层析。阴离子交换层析后活性回收率在１２０％左右。得到的产品经ＳＤＳ－ＰＡＧＥ银染为单一条带，比活可达１．５×１０￣７ｕ／ｍｇ。
Recombinant granulocyte-derived colony stimulating factor (rGM-CSF) is expressed in inclusion bodies in E. coli. On the basis of laboratory scale separation and purification, we conducted a pilot plant separation and purification study to optimize the fermentation, broken bacteria, inclusion body recovery, product extraction, renaturation, chromatographic separation and amplification process. According to the commonness of the expressed products of inclusion bodies, the first step of separation can remove most of the macromolecular impurities by molecular exclusion chromatography, and further purification schemes adopt anion exchange chromatography according to the molecular characteristics of the inclusion reagent lysis reagent and the product itself. After anion exchange chromatography activity recovery rate of about 120%. The resulting product by SDS-PAGE silver staining as a single band, specific activity up to 1.5 × 10 ~ 7u / mg.