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http://hdl.handle.net/10609/92408
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dc.contributor.authorCarr, Rachel-
dc.contributor.authorDi Bari, Lorenzo-
dc.contributor.authorLo Piano, Samuele-
dc.contributor.authorParker, David-
dc.contributor.authorPeacock, Robert D.-
dc.contributor.authorSanderson, John M.-
dc.date.accessioned2019-03-21T12:04:02Z-
dc.date.available2019-03-21T12:04:02Z-
dc.date.issued2012-02-13-
dc.identifier.citationCarr, R., Di Bari, L., Lo Piano, S., Parker, D., Peacock, R. D. & Sanderson, J. M. (2012). A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence. Dalton Transactions, 41(), 3154-13158. doi:10.1039/c2dt30143a-
dc.identifier.issn1477-9226MIAR
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dc.identifier.urihttp://hdl.handle.net/10609/92408-
dc.description.abstractReversible and selective binding of a dynamically racemic europium(III) complex to alpha-1-acid glycoprotein and alpha-1-antitrypsin is characterised by a significant change in the europium total emission spectral fingerprint and the switching on of a large circularly polarised luminescence (CPL) signal from the metal centre. Observation of an induced CD into the ligand chromophore in the presence of alpha-1-AGP allows a structure for the protein-bound complex to be postulated. A direct determination of elevated alpha-1-AGP levels in human serum was achieved by monitoring changes in the intensity ratio of Eu emission bands.-
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherDalton Transactions-
dc.relation.ispartofDalton Transactions, 41(),-
dc.relation.urihttp://dx.doi.org/10.1039/c2dt30143a-
dc.subjecteuropica
dc.subjectluminescènciaca
dc.subjectluminescenceen
dc.subjecteuropiumen
dc.subjecteuropioes
dc.subjectluminiscenciaes
dc.subject.lcshChemistryen
dc.titleA chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence-
dc.typeinfo:eu-repo/semantics/article-
dc.subject.lemacQuímica analíticaca
dc.subject.lcshesQuímica analíticaes
dc.rights.accessRightsinfo:eu-repo/semantics/closedAccess-
dc.identifier.doi10.1039/c2dt30143a-
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