BMP4重组蛋白在毕赤酵母中表达载体构建与纯化分析

Vector construction and purification analysis on recombinant BMP4 protein in Pichia pastoris

以骨形态发生蛋白(BMP4)为研究对象,将BMP4基因与IgG-Fc基因结合,改造成为BMP4-Fc融合蛋白,经巴斯德毕赤酵母诱导表达和DEAE阴离子纯化获得目的蛋白,并利用间充质干细胞验证了其生理活性.结果表明:使用巴斯德毕赤酵母能够很好表达BMP4-Fc融合蛋白,通过提纯条件,成功分离纯化BMP4-Fc融合蛋白,其生理活性达到商业化纯品水平,为BMP4生产与开发提供了新路径.

The paper research the BMP4-Fc fusion protein combined by the gene of bone morphogenetic protein-4 and the gene of the IgG-Fc fragment.The target protein was successfully expressed in Pichia pastoris and purified by DEAE anion.The activity was tested in mesenchymal stem cells.The results showed that Pichia pastoris could express BMP4-Fc fusion protein obviously.By optimizing the purification conditions, BPM4-Fc fusion protein can be successfully isolated and purified.Finally, we find that the physiological activity of BMP4 protein almost arrive the level of commercial pure product.The result of this paper might provide a new pathway for production and exploitation of BMP4 protein.