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Authordc.contributor.authorCampos, A. M. 
Authordc.contributor.authorLissi Gervaso, Eduardo A. 
Authordc.contributor.authorVergara, C. 
Authordc.contributor.authorLanio, M. E. 
Authordc.contributor.authorAlvarez, C. 
Authordc.contributor.authorPazos, I. 
Authordc.contributor.authorMorera, V. 
Authordc.contributor.authorGarcia, Y. 
Authordc.contributor.authorMartinez, D. 
Admission datedc.date.accessioned2018-12-20T15:10:04Z
Available datedc.date.available2018-12-20T15:10:04Z
Publication datedc.date.issued1999
Cita de ítemdc.identifier.citationProtein Journal, Volumen 18, Issue 3, 2018, Pages 297-306
Identifierdc.identifier.issn15723887
Identifierdc.identifier.issn15734943
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/158126
Abstractdc.description.abstractSt I is a toxin present in the Caribbean Sea anemone Stichodactyla helianthus which is highly hemolytic in the nanomolar concentration range. Exposure of the toxin to free radicals produced in the pyrolysis of 2,2′ -azobis(2-amidinopropane) hydrochloride leads to a progressive loss of hemolytic activity. This loss of hemolytic activity is accompanied by extensive modification of tryptophan residues. On the average, three tryptophan residues are modified by each inactivated toxin. The loss of hemolytic activity of St I takes place without significant changes in the protein structure, as evidenced by the similarity of the fluorescence and CD spectra of native and modified proteins. Also, the native and modified ensembles present a similar resistance to their denaturation by guanidinium chloride. The hemolytic behavior and the performance of the toxin at the single-channel level when incorporated to black lipid membranes suggest that the modified ensemble can be considered as composed of
Lenguagedc.language.isoen
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceProtein Journal
Keywordsdc.subjectHemolytic activity
Keywordsdc.subjectPeroxyl radicals
Keywordsdc.subjectSticholysin
Keywordsdc.subjectToxin
Títulodc.titleKinetics and mechanism of st i modification by peroxyl radicals
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile