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Authordc.contributor.authorCassels Niven, Bruce 
Cita de ítemdc.identifier.citationFASEB Journal, Volumen 11, Issue 9, 2018,
Abstractdc.description.abstractThe relationship between the free radical-induced loss of lysozyme activity and the occurrence of oxidative modifications, evidenced as gain in DNPHreactive carbonyl groups (CO) and loss of tryptophan-associated fluorescence (TAF), was addressed in vitro.2,2'-azobis (2-amidino propane)(20 raM, AAPtt) and a mixture of Fe+2/Ascorbate (Fe+2/A, 0.1/25 mM) were used as peroxyl and oxygen-de rived free radical sources. Lysozyme incubated (2h, 37C) in the presence of AAPH underwent a 75% decrease in its activity, a concomitant 50% loss of TAF, and a 6-fold rise in CO levels. Such a change in CO levels, however, could account at the most for the inactivation of 6% of the enzyme molecules. Further suggesting a dissociation between CO formation and inactivation, the enzyme's activity and the TAF remained totally unaltered upon exposure of the protein to Fe+2/A in spite of an almost 5-fold rise in CO. The effects induced by either AAPH or Fe+2/A were all inhibitable by antioxi dant addition. Neve
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.uri
Sourcedc.sourceFASEB Journal
Keywordsdc.subjectAgricultural and Biological Sciences (miscellaneous)
Keywordsdc.subjectBiochemistry, Genetics and Molecular Biology (all)
Keywordsdc.subjectCell Biology
Títulodc.titleLysozyme inactivation by free radicals can occur independently of reactive carbonyl formation
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación SCOPUS

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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