【摘要】 目的:纯化、复性猪干扰素-γ基因(poIFN-γ)表达产物并分析其抗病毒活性。方法:用异丙基-β-D-硫代半乳糖苷(Isopropylthio-β-D-galactoside,IPTG)诱导原核表达载体pQE30/poIFN-γ,超声裂解包涵体,尿素溶解、Ni-NTA纯化和透析复性后,对所得的蛋白进行抗病毒活性检测。结果:经复性纯化的目的蛋白纯度达95%以上,在PK15细胞上抗滤泡性口炎病毒比活性为6.2×105u/mg。结论:获得PoIFN-γ活性蛋白,为进一步研究应用奠定基础。更多还原

【Abstract】 Objective:To purify and renaturate poIFN-γ expressed product and to study its antiviral activity.Methods:After pQE30/poIFN-γ was induced with isopropye-β-D-thiogalactoside(IPTG),the inclusion bodies were isolated with sonicate,purified by using Ni-NTA agarose and renaturated with dialysis,then its antiviral activity was tested.Results:The purified protein reached about 95%.Its specific antiviral activity was about 6.2× 105u /mg on PK15/VSV test system.Conclusion:The active poIFN-γ protein has been obtained,which is a good fowndation for future research and application.更多还原