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Several serines present in transmembrane domain V are conserved among members of the G-protein-coupled receptor family that bind catecholamines. Two of these serines that are present in the beta-adrenergic receptor were previously shown by site-directed mutagenesis to affect agonist binding and receptor activation (Strader, C. D., Candelore, M. R., Hill, W.(More)
Receptors for dopamine are present on horizontal cells of fish retina that are linked to the activation of adenylate cyclase. In the present study, the goldfish (Carassius auratus) gene that encodes these receptors, referred to as gfD1, was isolated and analyzed. A single open reading frame within the gfD1 gene encodes a protein of 363 amino acids that is(More)
(-)-[3H]L364718 membrane binding assays were employed to localize and characterize cholecystokinin (CCK)-A binding sites in rat and cow brain. Specific binding was detected in all brain areas tested, but in all areas of rat brain and most areas of cow brain the level was too low to allow characterization of the ligand binding specificity of these sites.(More)
Dopamine is shown to stimulate cAMP accumulation in COS-1 cells via endogenously expressed dopamine D1 receptors. A dissociation of dopamine and beta-adrenoceptor responses is demonstrated by the use of selective antagonists and different desensitization patterns following exposure of the cells to dopamine or the beta-adrenoceptor agonist, isoproterenol.(More)
D1 and D2 dopamine receptors are G-protein coupled receptors and have seven transmembrane spanning regions (TM) typical of this receptor superfamily. Although dopamine binds equally to D1 and D2 receptors, many compounds are highly selective. To probe the receptors for regions that determine subtype specificity, plasmid constructs coding for the D1 or a(More)
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