title: Purification of oestradiol receptor from human uterus by affinity chromotrgraphy.
abstract: The oestrogen receptor from human myometrium has been extensively purified by affinity chromatography and isoelectric focusing. The latter step is necessary to remove contaminating sex-steroid-binding globulin. The unpurified 3.7-S cytoplasmic receptor has a molecular weight of 41,000, a Stokes radius of 27.0 A and a frictional ratio (f/f0) of 1.19; the KD (4 degrees C) for [3H]oestradiol-17 beta was 1.03 X 10(-10) M. After purification, the molecular weight was 30,000, the Stokes radius 23.6 A, frictional ratio 1.15 and isoelectric point 6.15.
mesh_terms: D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D004958:Estradiol / Q000378:metabolism*; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008722:Methods; D008970:Molecular Weight; D009215:Myometrium / Q000032:analysis* / Q000201:enzymology; D010447:Peptide Hydrolases / Q000378:metabolism; D011960:Receptors, Estrogen / Q000032:analysis / Q000302:isolation & purification*; D014599:Uterus / Q000032:analysis*
chemical_list: D011960:Receptors, Estrogen; D004958:Estradiol; D010447:Peptide Hydrolases