Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/12561
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dc.contributor.authorLiu, J Jen
dc.contributor.authorCasley, David Jen
dc.contributor.authorNayler, W Gen
dc.date.accessioned2015-05-16T02:16:30Z
dc.date.available2015-05-16T02:16:30Z
dc.date.issued1989-11-15en
dc.identifier.citationBiochemical and Biophysical Research Communications; 164(3): 1220-5en
dc.identifier.govdoc2556121en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/12561en
dc.description.abstractSpecific, high affinity binding sites for iodinated endothelin-1 ([125I]-ET-1) were identified in crude plasma and light membrane fractions harvested from aerobically perfused and ischaemic rat hearts, to determine whether the ischaemia-induced increase in binding site density (Bmax) involves externalization of the sites. In crude plasma membranes Bmax increased after 60 min ischaemia, from 113.5 +/- 2.15 to 180.6 +/- 4.67 fmol/mg protein (p less than 0.01). In the light membranes, the Bmax fell, from 94.7 +/- 8.70 to 63.80 +/- 6.26 fmol/mg protein (p less than 0.05). Hill coefficients and selectivity of both membrane fractions were unchanged. These results are interpreted as meaning that ischaemia causes externalization of cardiac [125I]-ET-1 binding sites.en
dc.language.isoenen
dc.subject.otherAerobiosisen
dc.subject.otherAnaerobiosisen
dc.subject.otherAnimalsen
dc.subject.otherBinding, Competitiveen
dc.subject.otherCell Fractionationen
dc.subject.otherCell Membrane.metabolismen
dc.subject.otherCoronary Disease.metabolismen
dc.subject.otherEndothelinsen
dc.subject.otherEndothelium, Vascularen
dc.subject.otherFemaleen
dc.subject.otherKineticsen
dc.subject.otherMaleen
dc.subject.otherMyocardium.metabolismen
dc.subject.otherPeptides.metabolismen
dc.subject.otherRatsen
dc.subject.otherRats, Inbred Strainsen
dc.subject.otherReceptors, Cell Surface.metabolismen
dc.subject.otherReceptors, Endothelinen
dc.subject.otherUltracentrifugationen
dc.titleIschaemia causes externalization of endothelin-1 binding sites in rat cardiac membranes.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.pages1220-5en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/2556121en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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