ISOLATION AND PHOTOOXIDATION OF LYSOZYME FRAGMENTS

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dc.contributor.authorFERRER, I
dc.contributor.authorSILVA, E
dc.date.accessioned2025-01-23T19:44:24Z
dc.date.available2025-01-23T19:44:24Z
dc.date.issued1981
dc.description.abstractReduction of the 4 disulfide bonds and further carboxymethylation of lysozyme followed by its reaction with CNBr brings about L-I, (aa [amino acids] 1-12) and L-II-III (aa 13-129) peptides. When breaking the polypeptidic chain by CNBr action and freeing the peptides formed through S-S bonds reduction and carboxymethylation, 3 peptides are obtained corresponding to L-I (aa 1-12), L-II (aa 13-105) and L-III (aa 106-129). L-II-III, L-III and L-II peptides were separately subjected to photo-oxidation in presence of riboflavin in 0.05 M phosphate buffer, pH 7.0. The kinetic analysis of Trp photo-oxidation in L-II-III peptides shows that these residues keep, to a great extent, the degree of exposure they had in native lysozyme. L-II peptide also presents Trp residues with a different degree of exposure. Presence of Tyr photo-oxidation in L-II and L-II-III peptides (this does not take place in native lysozyme) suggests a relationship between photo-oxidation selectivity and the degree of exposure of certain amino acid residues in spatial configuration.
dc.fuente.origenWOS
dc.identifier.eissn1432-2099
dc.identifier.issn0301-634X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/100030
dc.identifier.wosidWOS:A1981MV68500007
dc.issue.numero1
dc.language.isoen
dc.pagina.final77
dc.pagina.inicio67
dc.revistaRadiation and environmental biophysics
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleISOLATION AND PHOTOOXIDATION OF LYSOZYME FRAGMENTS
dc.typeartículo
dc.volumen20
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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