Tight binding of glucocorticoid-receptor complexes to histone-agarose.
"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.
Ueda
K
K
Department of Dermatology, Osaka University Medical School, Japan.
Isohashi
F
F
Okamoto
K
K
Kokuhu
I
I
Kimura
K
K
Yoshikawa
K
K
Sakamoto
Y
Y
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
D006657:Histones; D011965:Receptors, Glucocorticoid; D011732:Pyridoxal Phosphate; D014222:Triamcinolone Acetonide