Purification to homogeneity of the nuclear estrogen receptor from chick liver.
The nuclear estradiol receptor from chick liver was purified to apparent homogeneity by using a combination of ammonium sulfate precipitation and affinity gel chromatography. The purified receptor migrated as a single band on an SDS-polyacrylamide gel with a molecular weight of 55000 and it exhibited a sedimentation coefficient of 4 S, a dissociation constant of 1.13 nM and a steroid specificity resembling that of the receptor in crude extracts.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D002846:Chromatography, Affinity / Q000379:methods; D004958:Estradiol / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D011960:Receptors, Estrogen / Q000302:isolation & purification* / Q000378:metabolism
D011960:Receptors, Estrogen; D004958:Estradiol