Francavilla A, Eagon P K, DiLeo A, Van Thiel D H, Ove P, Wu S K, Sax S A, Starzl T E
Gastroenterology. 1984 Jun;86(6):1410-6.
Estrogen binding protein activities were determined in the cytosol from adult male Buffalo rat liver and Morris hepatoma 7777. Estrogen receptors were prepared using the protamine sulfate precipitation technique of Chamness. The ability of various unlabeled steroids competing with [3H]estradiol was examined to establish the binding specificity. Estradiol binding in Morris hepatoma 7777 cytosol was greatly decreased compared with that present in hepatic cytosol prepared from normal rat liver. The receptor concentration expressed as femtomoles per milligram of cytoplasmic protein was 31.1 +/- 2.9 SD for normal rat liver and 0.41 +/- 0.88 SD for the hepatoma. Gel filtration chromatography revealed the presence of an estrogen binder in hepatoma cytosol which was not present in either normal liver or in the protamine sulfate precipitates of hepatoma cytosol. The molecular weight, binding specificity, and precipitation of this protein by specific antiserum suggests that it is alpha-fetoprotein.
测定了成年雄性布法罗大鼠肝脏和莫里斯肝癌7777细胞溶质中的雌激素结合蛋白活性。采用查姆斯的硫酸鱼精蛋白沉淀技术制备雌激素受体。检测了各种未标记类固醇与[3H]雌二醇竞争的能力，以确定结合特异性。与正常大鼠肝脏制备的肝细胞溶质相比，莫里斯肝癌7777细胞溶质中的雌二醇结合显著降低。以飞摩尔每毫克细胞质蛋白表示的受体浓度，正常大鼠肝脏为31.1±2.9标准差，肝癌为0.41±0.88标准差。凝胶过滤色谱显示肝癌细胞溶质中存在一种雌激素结合剂，正常肝脏或肝癌细胞溶质的硫酸鱼精蛋白沉淀物中均不存在。该蛋白的分子量、结合特异性以及被特异性抗血清沉淀的特性表明它是甲胎蛋白。
