PHOTOCHEMICAL REACTIVITY OF THE HOMOLOGOUS PROTEINS ALPHA-LACTALBUMIN AND LYSOZYME

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dc.contributor.authorEDWARDS, AM
dc.contributor.authorSILVA, E
dc.date.accessioned2025-01-23T19:27:36Z
dc.date.available2025-01-23T19:27:36Z
dc.date.issued1985
dc.description.abstractThe fluorescent behavior and the photodynamic effect was studied in native and structurally modified lysozyme and .alpha.-lactalbumin. The Tyr residues in lysozyme and .alpha.-lactalbumin show different sensitivities to the photodynamic effect. The effect is zero in the case of Tyr from native lysozyme. In contrast, the Tyr residues in .alpha.-lactalbumin are susceptible to photooxidation, which indicates a greater degree of exposure to the solvent. The 3 His residues of .alpha.-lactalbumin have different degrees of exposure and show 2 different kinetics of photooxidation whereas the His residue of lysozyme is photooxidized with a single kinetic. Two photooxidation kinetics were obtained for the Trp residues of both native proteins, an indication that in both cases there are Trp residues that are differently exposed to the solvent. The wavelengths of maximum fluorescent emission of the Trp residues were different for the 2 proteins, an effect which can also be explained in terms of a difference in the environment of these residues. The modified form of these proteins emit at wavelengths longer than those of the native forms. When modified the proteins photooxidize with noticeably greater quantum yields.
dc.fuente.origenWOS
dc.identifier.eissn1432-2099
dc.identifier.issn0301-634X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99746
dc.identifier.wosidWOS:A1985AGN0900008
dc.issue.numero2
dc.language.isoen
dc.pagina.final148
dc.pagina.inicio141
dc.revistaRadiation and environmental biophysics
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titlePHOTOCHEMICAL REACTIVITY OF THE HOMOLOGOUS PROTEINS ALPHA-LACTALBUMIN AND LYSOZYME
dc.typeartículo
dc.volumen24
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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