用重组家蚕核多角体病毒（ｒＢｍＮＰＶ－ＩＦＮ－α）感染家蚕细胞，经ＳＰ－Ｓｅｐｈａｒｏｓｅ离子交换层析柱及单克隆抗体亲和层析，从细胞培养液中分离纯化α－干扰素，纯化倍数为１０１０，比活性为５．８７×１０８ＩＵ／ｍｇ蛋白，聚丙烯酰胺凝胶电冰呈单一条带，并用激光解离电离飞行质谱分析测定其分子量为２０４６５Ｄ，毛细管电泳鉴定纯度为９９．１％。表达产物Ｎ端１５个氨基酸分析结果与ＩＦＮ－α１ｃＤＮＡ推导的序列相同。 The silkworm cells were infected with recombinant Bombyx mori nucleopolyhedrovirus (rBmNPV-IFN-α), and the α-interferon was isolated and purified from the cell culture medium by SP-Sepharose ion exchange chromatography and monoclonal antibody affinity chromatography. The purification fold 1010, the specific activity of 5.87 × 108IU / mg protein, polyacrylamide gel electrophoresis was a single band, and the molecular mass was 20465D by laser desorption ionization mass spectrometry analysis, capillary electrophoresis identified purity of 99.1% . The N-terminal 15 amino acids of the expression product was analyzed in the same way as the IFN-α1 cDNA.