title: Tight binding of glucocorticoid-receptor complexes to histone-agarose.
abstract: "Activated" glucocorticoid-receptor complexes purified about 3,000-fold from rat liver were found to bind to histone-agarose. Because of their tight binding, they could not be eluted from the column by high salt solution (3 M KCl) or low salt plus polyol buffer (50% ethylene glycol), but their binding could be disrupted by pyridoxal 5'-phosphate; more than 70% recovery of the "activated" receptor complexes was achieved with buffer containing 20 mM pyridoxal 5'-phosphate. This interaction of "activated" glucocorticoid-receptor complexes of rat liver with histone-agarose suggests a role of histones in the mechanism of action of steroid hormone.
authors.affiliation: Department of Dermatology, Osaka University Medical School, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ueda
authors.forename: F
authors.initials: F
authors.lastname: Isohashi
authors.forename: K
authors.initials: K
authors.lastname: Okamoto
authors.forename: I
authors.initials: I
authors.lastname: Kokuhu
authors.forename: K
authors.initials: K
authors.lastname: Kimura
authors.forename: K
authors.initials: K
authors.lastname: Yoshikawa
authors.forename: Y
authors.initials: Y
authors.lastname: Sakamoto
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D002847:Chromatography, Agarose; D006657:Histones; D008099:Liver / Q000378:metabolism*; D011485:Protein Binding; D011732:Pyridoxal Phosphate; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification / Q000378:metabolism*; D014222:Triamcinolone Acetonide / Q000378:metabolism
chemical_list: D006657:Histones; D011965:Receptors, Glucocorticoid; D011732:Pyridoxal Phosphate; D014222:Triamcinolone Acetonide