Partial purification of rat liver glucocorticoid binding proteins by affinity chromatography.
Dexamethasone (9-fluoro-16alpha-methyl-11beta,17,21-trihydroxy-1,4-pregnadiene-3,20-dione) binding proteins from rat liver cytosol were purified approximately 6470 fold by the use of an affinity column in which deoxycorticosterone was linked to CH-Sepharose 4B through a disulfide linkage. The receptor proteins were eluted from the column by washing with beta-mercaptoethanol. A preliminary Sephadex G-200 filtration step of the cytosol was necessary in order to separate the dexamethasone binding proteins from other glucocorticoid receptors.
D000315:Adrenalectomy; D000818:Animals; D002846:Chromatography, Affinity; D003600:Cytosol / Q000378:metabolism; D003900:Desoxycorticosterone; D003907:Dexamethasone / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification* / Q000378:metabolism; D011987:Receptors, Steroid / Q000302:isolation & purification*
D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; D003900:Desoxycorticosterone; D003907:Dexamethasone