Study of a photo-induced lysozyme-riboflavin bond

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dc.contributor.authorFerrer Meli, Irene del Carmen
dc.contributor.authorSilva, E.
dc.date.accessioned2019-12-28T02:45:29Z
dc.date.available2019-12-28T02:45:29Z
dc.date.issued1985
dc.description.abstractIrradiation of lysozyme in the presence of riboflavin results in the formation of a lysozyme-riboflavin adduct. Reduction and carboxymethylation of the four disulfide bonds as well as the chemical modification of the Tyr residues and the photochemical alteration of the His residue in lysozyme, do not affect the formation of the photo-induced lysozyme-riboflavin bond. When the lysozyme-riboflavin adduct was subjected to mild acid hydrolysis and ion exchange chromatography, the retention of a compound containing14C-riboflavin was observed. Free14C-riboflavin, on the contrary is not retained by the column. The photo-oxidation of free Trp in the presence of14C-riboflavin, gave a compound which bound to the ion exchange resin like the above-mentioned derivative. The photo-oxidation of the Trp residues in lysozyme and in peptides obtained from lysozyme showed very high quantum yields, and these values were directly related to the incorporation of14C-riboflavin in these samples.
dc.fuente.origenSpringer
dc.identifier.doi10.1007/BF01212654
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/27132
dc.identifier.urihttp://link.springer.com/article/10.1007/BF01212654
dc.issue.numeroNo. 1
dc.language.isoen
dc.nota.accesoContenido parcial
dc.revistaRadiation and Environmental Biophysicses_ES
dc.rightsacceso restringido
dc.subject.ddc510
dc.subject.deweyMatemática física y químicaes_ES
dc.subject.otherDisúlfuroses_ES
dc.subject.otherLisozimaes_ES
dc.subject.otherHidrólisises_ES
dc.subject.otherFotoquímicaes_ES
dc.subject.otherBioquímica.es_ES
dc.titleStudy of a photo-induced lysozyme-riboflavin bondes_ES
dc.typeartículo
dc.volumenVol. 24
sipa.codpersvinculados49958
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