Interaction of chick oviduct progesterone receptor with immobilized aurintricarboxylic acid.
Aurintricarboxylic acid (ATA) was immobilized on Sepharose 4B via a carbodiimide coupling mechanism. A majority of the chick oviduct progesterone receptor was retained on the affinity resin and could be recovered upon washing the column with buffer containing free ligand or 3 M guanidine-HCl. The [3H]progesterone-receptor complex retained its integrity following the chromatography on ATA-Sepharose as judged by sedimentation analysis. The procedure allowed significant purification of progesterone receptor: SDS-polyacrylamide gel electrophoresis of the purified preparation revealed elimination of many peptide bands present in the cytosol prior to ATA-Sepharose chromatography. The technique thus has a clear potential in characterization and purification of progesterone receptor.
D000818:Animals; D001312:Aurintricarboxylic Acid / Q000378:metabolism*; D002846:Chromatography, Affinity / Q000379:methods; D003509:Cyclohexanecarboxylic Acids / Q000378:metabolism*; D003600:Cytosol / Q000032:analysis; D005260:Female; D008982:Molybdenum / Q000494:pharmacology; D010057:Oviducts / Q000032:analysis*; D011374:Progesterone / Q000378:metabolism; D011980:Receptors, Progesterone / Q000302:isolation & purification / Q000378:metabolism*
D003509:Cyclohexanecarboxylic Acids; D011980:Receptors, Progesterone; D001312:Aurintricarboxylic Acid; D011374:Progesterone; D008982:Molybdenum; C024687:sodium molybdate(VI)