Exposure of tryptophanyl residues inα-lactalbumin and lysozyme

Simple item page
dc.contributor.authorEdwardsM., Ana M
dc.contributor.authorSilva S., E.
dc.date.accessioned2019-12-28T02:45:32Z
dc.date.available2019-12-28T02:45:32Z
dc.date.issued1986
dc.description.abstractThe effect of iodide ion on the tryptophyl fluorescence of the homologous proteins lysozyme and?-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?-I (aa 1-90) from lysozyme and?-lactalbumin, respectively, showed Trp residues with different degree of exposure, whereas the smaller fragments, L-III (aa 106-129) and?-II (aa 91 123), had all their Trp residues exposed to the solvent.
dc.fuente.origenSpringer
dc.identifier.doi10.1007/BF01211735
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/27141
dc.identifier.urihttp://link.springer.com/article/10.1007/BF01211735
dc.issue.numeroNo. 2
dc.revistaRadiation and Environmental Biophysicses_ES
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.otherPéptidoses_ES
dc.subject.otherYoduroes_ES
dc.subject.otherLisozimaes_ES
dc.subject.otherBiofísicaes_ES
dc.titleExposure of tryptophanyl residues inα-lactalbumin and lysozymees_ES
dc.typeartículo
dc.volumenVol. 25
sipa.codpersvinculados53657
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Exposure of tryptophanyl residues in α-lactalbumin and lysozyme.pdf
Size:
153.15 KB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Artículos de revistas