Nuclear binding and sedimentation properties of two activated forms of glucocorticoid-receptor complexes from rat mammary glands.
Mammary cytoplasmic glucocorticoid-receptor complexes, which had been exposed to a high concentration of ammonium sulfate, were found to be separated into two receptor forms, consisting of DNA-cellulose-bound and non-DNA-cellulose-bound receptors. Experiments under cell-free conditions revealed that not only the DNA-cellulose-bound receptor but also the non-DNA-cellulose-bound receptor have binding abilities to nuclei and to nuclear chromatin. In sucrose density gradient centrifugation, the non-DNA-cellulose-bound receptor sedimented at higher sedimentation coefficients than the DNA-cellulose-bound receptor under all the salt conditions tested. These data strongly suggest that in the mammary glucocorticoid receptor system there exist at least two activated receptor forms with different conformations.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D003907:Dexamethasone / Q000378:metabolism; D005260:Female; D007700:Kinetics; D008321:Mammary Glands, Animal / Q000378:metabolism*; D008970:Molecular Weight; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; D003907:Dexamethasone