β-Adrenergic Receptor: Stereospecific Interaction of Iodinated β-Blocking Agent with High Affinity Site

作者：Gerald D. Aurbach, Susan A. Fedak, Charles Woodard, Jeffrey S. Palmer, Daniel Hauser, F. Troxler · 发表于：Science · 年份：1974 · DOI：10.1126/science.186.4170.1223 · 被引用次数：228 · 研究领域：Receptor Mechanisms and Signaling、Neuropeptides and Animal Physiology、Pharmacological Effects and Assays

An iodine-labeled beta-adrenergic inhibitor ((125)l-hydroxybenzylpindolol) binds specifically to a site on turkey erythrocyte membranes. A series of beta-adrenergic agonists and inhibitors compete for this binding site, with apparent affinities paralleling biological effectiveness as activators or inhibitors of catecholaminestimulated adenylate cyclase. The activity of d-(+) agonists or inhibitors was 1 percent (or less) than that of the corresponding l-(-) isomers in competing for binding of the iodinated blocker as well as in affecting catecholamine-stimulated adenylate cyclase. 1-(-)-Norepinephrine was about one-tenth as active as l-(-)-isoproterenol in competing for the beta-blocking agent site. The stereospecificity of the interaction with the iodinated beta-blocking agent and the correspondence between affinity for site and biological potency of analogs suggested that this interaction is involved in function of the beta-adrenergic receptor.