本研究利用本室建株的A_3 杂交瘤细胞株分泌的单克隆抗体,对大肠菌表达的人rIFN-γ进行了纯化。宿主菌经 7MGuHCl 处理后,收获的抽提液经 40％饱和(NH_4)_2SO_4盐析,除去部分杂蛋白,纯度约提高了一倍、活性回收>100％。此溶液稀释70倍复性后直接通过McAb亲和层析纯化,纯度达到98％,比活6×10~6Iu/mgp。本文还对复性的影响因素进行了研究,证实溶液的离子强度及蛋白浓度对复性均有影响。 In this study, the monoclonal antibody secreted by A_3 hybridoma cell line was used to purify human rIFN-γ expressed in Escherichia coli. The host bacteria after 7MGuHCl treatment, the harvested extract was 40% saturated (NH_4) _2SO_4 salting out to remove some of the impurities, the purity of about doubled the recovery of> 100%. This solution was diluted 70-fold renaturation and purified directly by McAb affinity chromatography with a purity of 98% and a specific activity of 6 × 10 ~ 6Iu / mgp. In this paper, the influence factors of refolding were also studied, and it was confirmed that the ionic strength and protein concentration of the solution all have influence on refolding.