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https://ahro.austin.org.au/austinjspui/handle/1/13025
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hogarth, P Mark | en |
dc.contributor.author | Ierino, F L | en |
dc.contributor.author | Hulett, M D | en |
dc.date.accessioned | 2015-05-16T02:47:57Z | |
dc.date.available | 2015-05-16T02:47:57Z | |
dc.date.issued | 1994-02-01 | en |
dc.identifier.citation | Immunomethods; 4(1): 17-24 | en |
dc.identifier.govdoc | 7520815 | en |
dc.identifier.other | PUBMED | en |
dc.identifier.uri | https://ahro.austin.org.au/austinjspui/handle/1/13025 | en |
dc.description.abstract | The 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.iso | en | en |
dc.subject.other | Amino Acid Sequence | en |
dc.subject.other | Animals | en |
dc.subject.other | Antibodies, Monoclonal | en |
dc.subject.other | Base Sequence | en |
dc.subject.other | Binding Sites | en |
dc.subject.other | Cell Line | en |
dc.subject.other | Epitopes.analysis | en |
dc.subject.other | Fluorescent Antibody Technique | en |
dc.subject.other | Humans | en |
dc.subject.other | Immunoglobulin G.metabolism | en |
dc.subject.other | Mice | en |
dc.subject.other | Molecular Sequence Data | en |
dc.subject.other | Oligonucleotides.chemistry | en |
dc.subject.other | Receptors, IgE.genetics.metabolism | en |
dc.subject.other | Receptors, IgG.genetics.metabolism | en |
dc.subject.other | Recombinant Fusion Proteins.genetics.metabolism | en |
dc.subject.other | Rosette Formation | en |
dc.subject.other | Transfection | en |
dc.title | Characterization of FcR Ig-binding sites and epitope mapping. | en |
dc.type | Journal Article | en |
dc.identifier.journaltitle | ImmunoMethods | en |
dc.identifier.affiliation | Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australia | en |
dc.description.pages | 17-24 | en |
dc.relation.url | https://pubmed.ncbi.nlm.nih.gov/7520815 | en |
dc.type.austin | Journal Article | en |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.fulltext | No Fulltext | - |
item.grantfulltext | none | - |
item.languageiso639-1 | en | - |
item.openairetype | Journal Article | - |
Appears in Collections: | Journal articles |
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