A β-Adrenergic Receptor of the Turkey Erythrocyte I. BINDING OF CATECHOLAMINE AND RELATIONSHIP TO ADENYLATE CYCLASE ACTIVITY

摘要: Abstract The interaction of catecholamines with the β-adrenergic receptor and activation adenylate cyclase were studied plasma membranes prepared from turkey erythrocytes. apparent affinity isoproterenol, determined by measuring [3H]isoproterenol, for was virtually identical Km isoproterenol. Binding catecholamine to necessary but not sufficient cyclase. dihydroxyphenyl function molecule required binding as well secondary alcohol at β-carbon, stereoconfiguration an amine function, primary or secondary, α-carbon functions essential specific catechol site. Those compounds that bound did stimulate effective inhibitors isoproterenol-stimulated activity. Propranolol, a blocker, potent inhibitor activity weak binding. It concluded in addition catechol-specific binding, further between membrane hormone is This appears involve site ethanolamine portion molecule.