文章基本信息

标题：Epinephrine Binding to the Catecholamine Receptor and Activation of the Adenylate Cyclase in Erythrocyte Membranes
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作者：M. Schramm ; H. Feinstein ; E. Naim 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：2
页码：523-527
DOI：10.1073/pnas.69.2.523
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Turkey erythrocyte membranes showed specific binding of [3H]epinephrine. The concentration of hormone required for half-maximal binding (30 {micro}M) was the same as that required for half-maximal activation of the adenylate cyclase located in the same membrane preparation. The binding reaction at 37{degrees}C reached completion during the first minute of incubation, which agrees well with the known rapidity of the biological response to catecholamines. Specific binding was abolished by heating the membranes 1 min at 100{degrees}C. Chromatography of the bound 3H, after its extraction from the membranes, indicated that the hormone had fully retained its chemical structure. Epinephrine binding was inhibited by the {beta}-adrenergic blocking agent propranolol, which also inhibited the activation of adenylate cyclase by the hormone. The specificity of phenethylamine derivatives in displacing [3H]epinephrine from the binding sites showed that a typical catecholamine receptor was responsible for the binding. Displacement of the bound hormone by analogs lacking the catechol group was more extensive at 37{degrees}C than at 0{degrees}C. Some of the analogs that displaced epinephrine from the binding site caused only a feeble activation of the adenylate cyclase, but were able to inhibit the activation of the enzyme by epinephrine. Thus, binding to a catecholamine receptor on a membrane preparation is an essential, but insufficient, condition to elicit a response.
关键词：hormone receptor ; β-adrenergic receptor ; cyclic AMP ; turkey