我们应用硫酸铵分段盐析,结合多种离子交换柱层析和羟磷灰石柱层析,从正常小鼠肝浸液中分离纯化出一种免疫抑制蛋白质,在体外它能很强地抑制小鼠T和B淋巴细胞对促有丝分裂原和同种异型抗原的增生反应。纯化的免疫抑制蛋白质经聚丙烯酰胺凝胶电泳及等电聚焦电泳鉴定均为一条带,其pI值在7.5～7.8之间。Sephadex G-100凝胶层析测得纯化蛋白质的分子量为78,000,SDS-PAGE测得此蛋白质亚基的分子量为38,500。同时经初步鉴定,此纯化的蛋白质既非糖蛋白又非脂蛋白。 We use ammonium sulfate segmented salting, combined with a variety of ion exchange column chromatography and hydroxyapatite column chromatography, isolated from normal mouse liver extract of an immunosuppressive protein, it can be very strong in vitro Inhibits the proliferative response of mouse T and B lymphocytes to mitogenic and allogenic antigens. Purified immunosuppressive proteins by polyacrylamide gel electrophoresis and isoelectric focusing electrophoresis were identified as a band, the pI value between 7.5 to 7.8. The molecular weight of the purified protein was 78,000 as determined by gel filtration chromatography on Sephadex G-100. The molecular weight of this protein subunit was 38,500 as determined by SDS-PAGE. At the same time, preliminary identification, the purified protein is neither glycoprotein nor lipoprotein.