Partial purification of a glucocorticoid receptor.
A simple method for purification of the glucocorticoid receptor from hepatoma tissue culture cells has been developed. The procedure, which requires only about 24 hr, involves biospecific adsorption of the receptor to deoxycorticosterone derivatized agarose, elution with a glucocorticoid, and gel filtration. The receptor-steroid complex is obtained in 35-40% yield and is about 2000-fold purified. It possesses properties similar to those reported in crude extracts, including sedimentation coefficient in glycerol gradients and activation-dependent binding to nuclei.
D001665:Binding Sites; D006528:Carcinoma, Hepatocellular / Q000032:analysis / Q000378:metabolism; D002460:Cell Line; D002846:Chromatography, Affinity; D003907:Dexamethasone / Q000378:metabolism; D005938:Glucocorticoids / Q000378:metabolism*; D008113:Liver Neoplasms; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D011956:Receptors, Cell Surface; D013760:Tetrahydrocortisol / Q000378:metabolism; D014222:Triamcinolone Acetonide / Q000378:metabolism
D005938:Glucocorticoids; D009363:Neoplasm Proteins; D011956:Receptors, Cell Surface; D013760:Tetrahydrocortisol; D003907:Dexamethasone; D014222:Triamcinolone Acetonide