Estrogen binding protein activity in Morris hepatoma 7777 compared with normal rat liver.
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.
D000818:Animals; D002850:Chromatography, Gel; D003600:Cytosol / Q000032:analysis; D008099:Liver / Q000032:analysis*; D008114:Liver Neoplasms, Experimental / Q000032:analysis*; D008297:Male; D011479:Protamines; D051381:Rats; D011960:Receptors, Estrogen / Q000032:analysis*; D014316:Tritium; D000509:alpha-Fetoproteins / Q000032:analysis
D011479:Protamines; D011960:Receptors, Estrogen; D000509:alpha-Fetoproteins; D014316:Tritium