应用疏水层析纯化HIV-1跨膜蛋白gp41截短体包涵体

Purification of Inclusion Body of HTV-1 Transmembrane Protein gp41 Truncate by Hydrophobic Chromatography

目的对表达HIV-1跨膜蛋白gp41截短体包涵体进行纯化。方法将收获的表达菌体洗涤、超声波破菌、预处理后进行疏水层析。结果纯化后的gp41截短体的融合蛋白纯度达到90％,并且具有较好的抗原性和特异性。结论利用疏水层析可以将目的蛋白进行有效的纯化,为下一步的应用打下基础。

Objective To purify the inclusion body of expressed HIV-1 transmembrane protein gp41 truncate. Methods Ultrasonicate the expressed bacteria and purify the inclusion body by hydrophobic chrom-atography. Results The fusion protein of gp41 truncate obtained by the purification of inclusion body reached a purity of 90% and showed good antigenicity and specificity. Conclusion The HTV-1 transmembrane protein gp41 truncate protein was effectively purified by hydrophobic chromatography.