Estrogen receptor from human breast cancer and from normal human uterus: isolation and characterization of similar binding complexes.
Estrogen receptor from human breast cancer tissue and from normal human uterus was isolated and characterized by a combination of physical separation methods including ammonium sulfate precipitation, gel permeation chromatography, isoelectric focusing and gel electrophoresis. After incubation with 3H-estradiol-17 beta (3HE2) followed by gel permeation chromatography, specific estrogen-binding activity was found to be present in a 160,000-dalton molecular weight component which had a pI of 7.1-7.3. On polyacrylamide gel electrophoresis this estrogen-binding protein migrated as a single band which could however be dissociated into two subunits with molecular weights of +/- 60,000 and +/- 75,000 daltons. 3HE2 binding was to the 75,000-dalton component.
D000645:Ammonium Sulfate; D001943:Breast Neoplasms / Q000378:metabolism*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003600:Cytosol / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D011960:Receptors, Estrogen / Q000302:isolation & purification*; D014599:Uterus / Q000378:metabolism*
D011960:Receptors, Estrogen; D000645:Ammonium Sulfate