LIGHT-INDUCED BINDING OF RIBOFLAVIN TO LYSOZYME

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dc.contributor.authorSILVA, E
dc.contributor.authorGAULE, J
dc.date.accessioned2025-01-23T19:44:55Z
dc.date.available2025-01-23T19:44:55Z
dc.date.issued1977
dc.description.abstractPhotodynamic inactivation of lysozyme in air saturated H2O and D2O (phosphate buffer 0.05 M, pH 7.0) in the presence of methylene blue and riboflavin was studied. When H2O was replaced by D2O a great increase in rate of photoinactivation of lysozyme was observed. Photooxidation was inhibited by singlet oxygen quenchers like NaN3, and these reactions may have occurred via a singlet oxygen mechanism. Riboflavin was strongly bound to the enzyme as a result of illumination. A higher quantum was observed when riboflavin was used, although this dye was bleached during irradiation.
dc.fuente.origenWOS
dc.identifier.eissn1432-2099
dc.identifier.issn0301-634X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/100157
dc.identifier.wosidWOS:A1977EF55400005
dc.issue.numero4
dc.language.isoen
dc.pagina.final310
dc.pagina.inicio303
dc.revistaRadiation and environmental biophysics
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleLIGHT-INDUCED BINDING OF RIBOFLAVIN TO LYSOZYME
dc.typeartículo
dc.volumen14
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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