Purification of Glucocorticoid Receptor from Rabbit Liver by Steroid Affinity Chromatography

Abstract The glucocorticoid receptor from rabbit liver cytosol was partially purified by a two step procedure. Unbound receptor was precipitated with protamine sulfate and the extractum treated by affinity chromatography using a dexamethasone derivatized agarose. At this step a 2000-fold purification with 20-30% yield was achieved. Further purification was obtained by ion exchange chromatography or size exclusion HPLC. The homogeneity of the different eluates were tested by SDS polyacrylamide electrophoresis. Physicochemical analysis of receptor in cytosol and after purification revealed that it still remained in its “non transformed” state.