EXPOSURE OF TRYPTOPHANYL RESIDUES IN ALPHA-LACTALBUMIN AND LYSOZYME - QUANTITATIVE-DETERMINATION BY FLUORESCENCE QUENCHING STUDIES

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dc.contributor.authorEDWARDS, AM
dc.contributor.authorSILVA, E
dc.date.accessioned2025-01-23T19:26:42Z
dc.date.available2025-01-23T19:26:42Z
dc.date.issued1986
dc.description.abstractThe effect of iodide ion on the tryptophyl fluorescence of the homologous proteins lysozyme and .alpha.-lactalbumin in their native form, as well as in their modified structures and in fragments from these proteins was studied. By assessing the contribution to the total fluorescence of the exposed and buried Trp residues, and of the respective fluorescence quantum yields, the quantization of the number of Trp exposed to the solvent for all the species studied was possible. Both native proteins show an important increase in the number of Trp residues exposed to the solvent when treated with denaturing agents. The peptides L-II (aa 13-105) and .alpha.-I (aa 1-90) from lysozyme and .alpha.-lactalbumin, respectively, showed Trp residues with different degree of exposure, whereas the smaller fragments, L-III (aa 106-129) and .alpha.-II (aa 91-123), had all their Trp residues exposed to the solvent.
dc.fuente.origenWOS
dc.identifier.eissn1432-2099
dc.identifier.issn0301-634X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99644
dc.identifier.wosidWOS:A1986D752900004
dc.issue.numero2
dc.language.isoen
dc.pagina.final122
dc.pagina.inicio113
dc.revistaRadiation and environmental biophysics
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleEXPOSURE OF TRYPTOPHANYL RESIDUES IN ALPHA-LACTALBUMIN AND LYSOZYME - QUANTITATIVE-DETERMINATION BY FLUORESCENCE QUENCHING STUDIES
dc.typeartículo
dc.volumen25
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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