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Article: Effects of GTP on binding of [ 3H]glucagon to receptors in rat hepatic plasma membranes

TitleEffects of GTP on binding of [ 3H]glucagon to receptors in rat hepatic plasma membranes
Authors
Issue Date1977
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1977, v. 252 n. 8, p. 2790-2792 How to Cite?
AbstractIn this study, we report the preparation of [ 3H]glucagon and its characteristics of binding to receptors in the rat liver plasma membrane. Binding of the labeled hormone is optimal at pH 7.0. In the absence of GTP, [ 3H]glucagon binding to receptors is slow and the time of equilibration is inversely proportional to the hormone concentration. In the presence of GTP, equilibrium is reached within 30 s regardless of hormone levels, and the kinetics of binding are in accord with the kinetics of activation of adenylate cyclase by native glucagon in the presence of the nucleotide. Equilibrium binding measurements indicate that, in the absence of GTP, the binding isotherm is sigmoidal with an apparent K(d) of 2 nM. The addition of GTP results in a complex binding isotherm with about 90% of the binding sites having a considerably lower apparent dissociation constant (>10 nM) and a small population of sites having high affinity for the hormone. The binding properties of [ 3H]glucagon are compared with those of 125I-glucagon, and the implications of the actions of GTP on glucagon binding are discussed in relation to the overall regulation of adenylate cyclase by hormone and the nucleotide.
Persistent Identifierhttp://hdl.handle.net/10722/167442
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorNicosia, Sen_US
dc.contributor.authorLad, PMen_US
dc.contributor.authorRodbell, Men_US
dc.date.accessioned2012-10-08T03:07:02Z-
dc.date.available2012-10-08T03:07:02Z-
dc.date.issued1977en_US
dc.identifier.citationJournal Of Biological Chemistry, 1977, v. 252 n. 8, p. 2790-2792en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/167442-
dc.description.abstractIn this study, we report the preparation of [ 3H]glucagon and its characteristics of binding to receptors in the rat liver plasma membrane. Binding of the labeled hormone is optimal at pH 7.0. In the absence of GTP, [ 3H]glucagon binding to receptors is slow and the time of equilibration is inversely proportional to the hormone concentration. In the presence of GTP, equilibrium is reached within 30 s regardless of hormone levels, and the kinetics of binding are in accord with the kinetics of activation of adenylate cyclase by native glucagon in the presence of the nucleotide. Equilibrium binding measurements indicate that, in the absence of GTP, the binding isotherm is sigmoidal with an apparent K(d) of 2 nM. The addition of GTP results in a complex binding isotherm with about 90% of the binding sites having a considerably lower apparent dissociation constant (>10 nM) and a small population of sites having high affinity for the hormone. The binding properties of [ 3H]glucagon are compared with those of 125I-glucagon, and the implications of the actions of GTP on glucagon binding are discussed in relation to the overall regulation of adenylate cyclase by hormone and the nucleotide.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding, Competitiveen_US
dc.subject.meshCell Membrane - Drug Effects - Metabolismen_US
dc.subject.meshGlucagon - Metabolismen_US
dc.subject.meshGuanosine Triphosphate - Pharmacologyen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshKineticsen_US
dc.subject.meshLiver - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshReceptors, Cell Surface - Drug Effects - Metabolismen_US
dc.titleEffects of GTP on binding of [ 3H]glucagon to receptors in rat hepatic plasma membranesen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid16000-
dc.identifier.scopuseid_2-s2.0-0017647745en_US
dc.identifier.volume252en_US
dc.identifier.issue8en_US
dc.identifier.spage2790en_US
dc.identifier.epage2792en_US
dc.identifier.isiWOS:A1977DD63900049-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridNicosia, S=7102299447en_US
dc.identifier.scopusauthoridLad, PM=7006446792en_US
dc.identifier.scopusauthoridRodbell, M=7006658086en_US

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