Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11254
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dc.contributor.authorLiu, J Jen
dc.contributor.authorKelly, Jen
dc.contributor.authorCasley, David Jen
dc.contributor.authorJohnston, Colin Ien
dc.contributor.authorNayler, W Gen
dc.date.accessioned2015-05-16T00:50:35Z
dc.date.available2015-05-16T00:50:35Z
dc.date.issued1990-01-15en
dc.identifier.citationBiochemical and Biophysical Research Communications; 166(1): 299-307en
dc.identifier.govdoc2154201en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/11254en
dc.description.abstractAdult rat cardiac endothelin-1 (ET-1) receptors were solubilized with 0.5% digitonin and then characterized. The receptors retained binding activity after solubilization. Binding was saturable (KD of 0.065 +/- 0.004 nM, Bmax of 94.6 +/- 4.5 fmol/mg protein; Hill coefficient of 0.987 +/- 0.017 n = 6) and pH dependent, with the binding increasing as the pH was decreased from 10 to 4, but decreasing dramatically as pH dropped to 2. Specifically bound [125I]-ET-1 was not dissociated by 2 x 10(-7) M unlabelled ET-1, but was dissociated by pH 10 and 2. Returning the pH to 7.4 restored the binding activity of the receptors. Unlabelled ET-1 (10(-12) - 10(-7) M) and sarafotoxin S6b(10(-12) - 10(-7) M) competed with [125I]-ET-1 for binding to the receptors.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherBinding, Competitiveen
dc.subject.otherCell Membrane.metabolismen
dc.subject.otherDigitoninen
dc.subject.otherEndothelinsen
dc.subject.otherEndothelium, Vascularen
dc.subject.otherFemaleen
dc.subject.otherHydrogen-Ion Concentrationen
dc.subject.otherKineticsen
dc.subject.otherMyocardium.metabolismen
dc.subject.otherPeptides.metabolismen
dc.subject.otherRatsen
dc.subject.otherRats, Inbred Strainsen
dc.subject.otherReceptors, Cell Surface.isolation & purification.metabolismen
dc.subject.otherReceptors, Endothelinen
dc.titleSolubilization and characterization of endothelin-1 receptors in rat cardiac tissue.en
dc.typeJournal Articleen
dc.identifier.journaltitleBiochemical and biophysical research communicationsen
dc.identifier.affiliationDepartment of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages299-307en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/2154201en
dc.type.austinJournal Articleen
item.grantfulltextnone-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
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