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目的 获得高纯度和高活性的B淋巴细胞刺激因子。方法 重组原核表达载体pQE 80L BLyS112 -2 85在大肠杆菌DH5α中经IPTG诱导表达rhBLyS112 -2 85,超声碎菌 ,提取包涵体 ,经Ni2 + NTA亲和层析和SepharcrylS 2 0 0凝胶过滤层析纯化后 ,选择不同氧化还原条件进行复性 ,进而检测其生物学活性。结果 得到了有较高纯度和较好生物学活性的rhBLyS112 -2 85蛋白。结论 优化了BLyS蛋白的纯化和复性的参数 ,所获结果为进一步研究创造了条件
Objective To obtain high purity and high activity of B lymphocyte stimulating factor. Methods Recombinant prokaryotic expression vector pQE80L BLyS112 -2 85 was induced by IPTG in E. coli DH5α to induce rhBLyS112 -2 85. The inclusion bodies were extracted and purified by N 2 + NTA affinity chromatography and Sephacryl S 20 0 gel filtration After purification, the different redox conditions were selected for renaturation, and then the biological activity was tested. As a result, rhBLyS112 -285 protein with higher purity and better biological activity was obtained. Conclusion The parameters of purification and renaturation of BLyS protein were optimized, and the results obtained provided the conditions for further research