Partial purification of rat liver glucocorticoid binding proteins by affinity chromatography

Abstract

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.