重组人干细胞因子/血小板生成素融合蛋白的纯化及复性研究

Purification and renaturation of recombinant human SCF-TPO fusion protein

目的 探讨重组人干细胞因子/血小板生成素(SCF TPO)融合蛋白纯化及复性的最佳方法。方法 裂解 法提取包涵体,在变性条件下利用金属螯和层析获得融合蛋白,经透析及谷胱甘肽氧化还原法对纯化的融合蛋白进 行复性。结果 获得具有初步生物学活性的SCF TPO融合蛋白,其纯度高达90%。结论 该纯化方法操作简捷, 特异性高,纯化效果好,获得率高。

Objective To study the purification and renaturation of recombinant human SCF-TPO fusion protein. Methods After the inclusion bodies were isolated, the optimal conditions for denaturation and renaturation were studied. The denatured recombinant human SCF-TPO fusion protein was purified by metal chelating chromatography and renatured by dialysis in GSH/GSSH. Results The purified SCF-TPO fusion protein manifested primary biological activity with a purity of up to 90%. Conclusion The purification procedures employed in this study is simple and reliable, with a high specificity and good purification rate.