Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13025
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dc.contributor.authorHogarth, P Marken
dc.contributor.authorIerino, F Len
dc.contributor.authorHulett, M Den
dc.date.accessioned2015-05-16T02:47:57Z
dc.date.available2015-05-16T02:47:57Z
dc.date.issued1994-02-01en
dc.identifier.citationImmunomethods; 4(1): 17-24en
dc.identifier.govdoc7520815en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/13025en
dc.description.abstractThe low-affinity receptor for IgG, Fc gamma RII, and the high-affinity receptor for IgE, Fc epsilon RI, are functionally distinct but structurally homologous receptors. These characteristics have been exploited using a chimeric receptor strategy to examine segments of human Fc gamma RII for IgG-binding function. A series of chimeric receptors was generated by exchanging coding regions of the extracellular ligand-binding regions between Fc gamma RII and the Fc epsilon RI alpha chain using splice overlap extension by the polymerase chain reaction. The expression of these chimeric receptors in COS-7 cells and analysis of their IgG/IgE binding capacities have enabled the Ig-binding region of Fc gamma RII to be localized to a subregion of the second extracellular domain. The localization of the Ig-binding region of Fc gamma RII has provided the opportunity of performing site-directed mutagenesis to determine the key amino acids involved in the interaction of the receptor with IgG. These findings demonstrate that the chimeric receptor approach is a powerful technique for the dissection of structure/function relationships of structurally related yet functionally different molecules.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherAntibodies, Monoclonalen
dc.subject.otherBase Sequenceen
dc.subject.otherBinding Sitesen
dc.subject.otherCell Lineen
dc.subject.otherEpitopes.analysisen
dc.subject.otherFluorescent Antibody Techniqueen
dc.subject.otherHumansen
dc.subject.otherImmunoglobulin G.metabolismen
dc.subject.otherMiceen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherOligonucleotides.chemistryen
dc.subject.otherReceptors, IgE.genetics.metabolismen
dc.subject.otherReceptors, IgG.genetics.metabolismen
dc.subject.otherRecombinant Fusion Proteins.genetics.metabolismen
dc.subject.otherRosette Formationen
dc.subject.otherTransfectionen
dc.titleCharacterization of FcR Ig-binding sites and epitope mapping.en
dc.typeJournal Articleen
dc.identifier.journaltitleImmunoMethodsen
dc.identifier.affiliationAustin Research Institute, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages17-24en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/7520815en
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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