STUDY OF A PHOTOINDUCED LYSOZYME-RIBOFLAVIN BOND
dc.contributor.author | FERRER, I | |
dc.contributor.author | SILVA, E | |
dc.date.accessioned | 2025-01-23T19:27:09Z | |
dc.date.available | 2025-01-23T19:27:09Z | |
dc.date.issued | 1985 | |
dc.description.abstract | Irradiation of lysozyme in the presence of riboflavin results in the formation of a lysozyme-riboflavin adduct. Reduction and carboxymethylation of the 4 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 containing 14C-riboflavin was observed. Free 14C-riboflavin, on the contrary, is not retained by the column. The photo-oxidation of free Trp in the presence of 14C-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 of 14C-riboflavin in these samples. | |
dc.fuente.origen | WOS | |
dc.identifier.eissn | 1432-2099 | |
dc.identifier.issn | 0301-634X | |
dc.identifier.uri | https://repositorio.uc.cl/handle/11534/99696 | |
dc.identifier.wosid | WOS:A1985AHJ1100007 | |
dc.issue.numero | 1 | |
dc.language.iso | en | |
dc.pagina.final | 70 | |
dc.pagina.inicio | 63 | |
dc.revista | Radiation and environmental biophysics | |
dc.rights | acceso restringido | |
dc.subject.ods | 03 Good Health and Well-being | |
dc.subject.odspa | 03 Salud y bienestar | |
dc.title | STUDY OF A PHOTOINDUCED LYSOZYME-RIBOFLAVIN BOND | |
dc.type | artículo | |
dc.volumen | 24 | |
sipa.index | WOS | |
sipa.trazabilidad | WOS;2025-01-12 |