Binding of (125I)iodohydroxybenzylpindolol to putative beta-adrenergic receptors of rat glioma cells and other cell clones.
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TLDR
While most compounds that interacted with the beta-adrenergic receptor also influenced binding to the second site, the latter did not distinguish between stereoisomers of propranolol, and its affinity for the other compounds tested was poorer.About:
This article is published in Journal of Biological Chemistry.The article was published on 1976-03-10 and is currently open access. It has received 213 citations till now. The article focuses on the topics: Cyclase activity & Ligand (biochemistry).read more
Citations
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Relationship between the beta-adrenergic receptor and adenylate cyclase.
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Reconstitution of hormone-sensitive adenylate cyclase activity with resolved components of the enzyme.
TL;DR: The thermostable moiety of the enzyme appears to consist of two functional components, based upon differential thermal lability of its ability to reconstitute hormone-, NaF-, or Gpp(NH)p-stimulated adenylate cyclase activity.
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(+/-)[125Iodo] cyanopindolol, a new ligand for beta-adrenoceptors: identification and quantitation of subclasses of beta-adrenoceptors in guinea pig.
TL;DR: The low dissociation constant of ICYP in combination with its high specific radioactivity allows binding studies to be carried out with small protein and ligand concentrations, e.g. 3 μg protein per assay in guinea pig lung membranes.
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Dopaminergic receptors in the anterior pituitary gland. Correlation of [3H]dihydroergocryptine binding with the dopaminergic control of prolactin release.
Marc G. Caron,M. Beaulieu,Vincent Raymond,B Gagné,Jacques Drouin,Robert J. Lefkowitz,Fernand Labrie +6 more
TL;DR: The ergot alkaloid, a potent dopaminergic agonist, has been used to study binding sites in bovine anterior pituitary membranes and fulfilled another criterion of specific receptor sites in that binding to the anterior pituitsary sites was saturable with an apparent dissociation constant.
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Regulation of beta-adrenergic receptors by guanyl-5'-yl imidodiphosphate and other purine nucleotides.
TL;DR: Results appear to indicate that conformational alterations in adenylate cyclase caused by occupation of nucleotide regulatory sites by Gpp(NH)p are capable of inducing alterations in the beta-adrenergic receptors.
References
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A Protein Binding Assay for Adenosine 3′:5′-Cyclic Monophosphate
TL;DR: A simple and sensitive assay for adenosine 3':5'-cyclic monophosphate (cAMP) has been developed that is based on competition for protein binding of the nucleotide, presumably to a cAMP-dependent protein kinase.
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Stereospecific (3H)(minus)-alprenolol binding sites, beta-adrenergic receptors and adenylate cyclase.
TL;DR: The binding of [ 3 H]-alprenolol (a potent β-adrenergic antagonist) to sites in frog erythrocyte membranes has been studied by a centrifugal assay as discussed by the authors.
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β - Adrenergic Receptor: Stereospecific Interaction of Iodinated β - Blocking Agent with High Affinity Site
TL;DR: The stereospecificity of the interaction with the iodinated β-blocking agent and the correspondence between affinity for site and biological potency of analogs suggested that this interaction is involved in function of the β-adrenergic receptor.
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Identification of cardiac beta-adrenergic receptors by (minus) [3H]alprenolol binding
TL;DR: (Minus) [3-H] alprenolol, a potent beta-adrenergic antagonist, was used to identify binding sites in a fraction of canine cyocardium, suggesting that these binding sites represent the cardiac beta- adrenergic receptors.
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A beta-adrenergic receptor of the turkey erythrocyte. I. Binding of catecholamine and relationship to adenylate cyclase activity.
TL;DR: It was concluded that in addition to catechol-specific binding, a further interaction between plasma membrane and hormone is necessary for activation of adenylate cyclase, and this further interaction appears to involve a site specific for the ethanolamine portion of thecatecholamine molecule.