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dc.contributor.authorGalaris, D.en
dc.contributor.authorMira, D.en
dc.contributor.authorSevanian, A.en
dc.contributor.authorCadenas, E.en
dc.contributor.authorHochstein, P.en
dc.date.accessioned2015-11-24T19:27:09Z-
dc.date.available2015-11-24T19:27:09Z-
dc.identifier.issn0003-9861-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/22788-
dc.rightsDefault Licence-
dc.subjectCholesterol/*metabolismen
dc.subjectChromatography, High Pressure Liquiden
dc.subjectFatty Acids, Unsaturated/metabolismen
dc.subjectHemeproteins/*metabolismen
dc.subjectHydrogen Peroxide/*pharmacologyen
dc.subjectLipid Peroxides/metabolismen
dc.subjectLuminescent Measurementsen
dc.subjectMetmyoglobin/*metabolismen
dc.subjectOxidation-Reductionen
dc.subjectSalicylic Aciden
dc.subjectSalicylic Acids/*metabolismen
dc.subjectTime Factorsen
dc.titleCo-oxidation of salicylate and cholesterol during the oxidation of metmyoglobin by H2O2en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/3355168-
heal.identifier.secondaryhttp://www.sciencedirect.com/science/article/pii/0003986188901841-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1988-
heal.abstractThe reaction between metmyoglobin and H2O2 proceeds with oxidation of the hemo-protein iron to a higher valence state and consumption of the peroxide. This reaction is further associated with (a) O2 evolution; (b) hydroxylation of the aromatic compound salicylate to yield a set of dihydroxybenzoic acid derivatives (analyzed by HPLC with electrochemical detection); (c) autoxidation of cholesterol with formation of 3 beta-hydroxy-5-alpha-cholest-6-ene-5-hydroperoxide; and (d) formation of electronically excited states detected by low-level chemiluminescence. The heterolytic scission of the O-O bond of hydroperoxides by metmyoglobin causes the formation of an oxidizing equivalent capable of promoting peroxidation of linoleate and arachidonate (as indicated by the parallel formation of thiobarbituric acid-reactive material and an enhancement of chemiluminescence intensity). The identity of the oxidizing equivalent(s) is discussed in terms of the formation of a relatively stable higher state of oxidation of heme Fe (FeIV-OH or FeV = O) as well as on possible intermediate species derived during the decomposition of H2O2 by metmyoglobin, such as HO.and 1O2. These species might be involved either simultaneously or sequentially in the peroxidation of fatty acids as well as in the tissue damage associated with the formation of H2O2 in ischemic-reperfusion states.en
heal.journalNameArch Biochem Biophysen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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