Chanderbhan R, Tanaka T, Strauss J F, Irwin D, Noland B J, Scallen T J, Vahouny G V
Biochem Biophys Res Commun. 1983 Dec 28;117(3):702-9. doi: 10.1016/0006-291x(83)91654-6.
Purified sterol carrier protein2 (SCP2) from rat liver stimulated utilization of endogenous cholesterol for pregnenolone synthesis by adrenal mitochondria. Cytosolic preparations of rat liver, adrenal and luteinized ovary were also stimulatory in mitochondrial pregnenolone synthesis to different extents. Treatment of all preparations with rabbit anti-rat SCP2 IgG neutralized the stimulatory effects, and immunoprecipitated proteins gave similar patterns on SDS-gradient polyacrylamide gel electrophoresis. Treatment with rabbit pre-immune IgG had no effect on these parameters. Thus, proteins which are immunochemically compatible with hepatic SCP2 appear to be present in steroidogenic tissues and may play a role in control of mitochondrial cholesterol side chain cleavage activity.
从大鼠肝脏中纯化得到的固醇载体蛋白2（SCP2）可刺激肾上腺线粒体利用内源性胆固醇合成孕烯醇酮。大鼠肝脏、肾上腺和黄体化卵巢的胞质制剂对线粒体孕烯醇酮合成也有不同程度的刺激作用。用兔抗大鼠SCP2 IgG处理所有制剂可中和其刺激作用，并且免疫沉淀的蛋白在SDS梯度聚丙烯酰胺凝胶电泳上呈现相似的图谱。用兔免疫前IgG处理对这些参数没有影响。因此，与肝脏SCP2免疫化学性质相符的蛋白似乎存在于类固醇生成组织中，并且可能在控制线粒体胆固醇侧链裂解活性中发挥作用。
