A β-Adrenergic Receptor of the Turkey Erythrocyte II. CHARACTERIZATION AND SOLUBILIZATION OF THE RECEPTOR

摘要: Abstract The stability of the catechol-specific β-adrenergic receptor turkey erythrocytes was tested with certain physical and chemical agents. for catechol function stable at high temperatures or to treatment ultrasound. Phospholipase, Pronase, trypsin, Triton X-100, sodium lauryl sulfate, Lubrol-PX destroyed catecholamine-sensitive adenylate cyclase but not catecholamine-specific binding. Exposure trypsin released from membrane. solubilized material did sediment 100,000 x g showed properties virtually identical on cell Association dissociation rates, agents, Km catecholamine binding were all similar particulate receptor. It concluded that by represents fraction site.