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中文摘要：
用蛋白折叠液相色谱法（PFLC）对大肠杆菌表达的包涵体形式的重组人粒细胞集落刺激因子（rhG-CSF）进行了复性并同时纯化。用Cu^2＋-亚氨基二乙酸（IDA）Sepharose作为固定化金属离子亲和色谱的固定相。在低浓度脲存在下,以咪唑为洗脱剂,采用线性梯度洗脱rhG-CSF。该法仅通过一步PFLC分离,减少了复性过程中rhG-CSF的聚集,复性后的rhG-CSF的比活性为1.8×10^8IU/mg,纯度为97%,质量回收率为32%。
英文摘要：
Recombinant human granulocyte colony-stimulating factor （rhG-CSF） in the form of inclusion bodies expressed in Escherichia coli （E. coli） was simultaneously refolded and purified using protein folding liquid chromatography （PFLC）. Cu^2＋ -iminodiacetic acid （IDA） Sepharose was selected as the stationary phase for immobilized metal ion affinity chromatography. rhG-CSF was purified and the aggregates were diminished under a linear gradient elution of im-idazole in the presence of a suitable concentration of urea. Using only one PFLC run, the re-folded rhG-CSF had a specific bioactivity of 1.8 × 108 IU/mg and a purity of 97% , with the mass recovery of 32%.
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