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Iron-ethylenediaminetetraacetic acid (EDTA)-catalyzed superoxide dismutation revisited: An explanation of why the dismutase activity of Fe-EDTA cannot be detected in the cytochrome c/xanthine oxidase assay system

dc.contributor.authorBull, C.en_US
dc.contributor.authorFee, James A.en_US
dc.contributor.authorO'Neill, P.en_US
dc.contributor.authorFielden, E. M.en_US
dc.date.accessioned2006-04-07T17:52:42Z
dc.date.available2006-04-07T17:52:42Z
dc.date.issued1982-05en_US
dc.identifier.citationBull, C., Fee, J. A., O'Neill, P., Fielden, E. M. (1982/05)."Iron-ethylenediaminetetraacetic acid (EDTA)-catalyzed superoxide dismutation revisited: An explanation of why the dismutase activity of Fe-EDTA cannot be detected in the cytochrome c/xanthine oxidase assay system." Archives of Biochemistry and Biophysics 215(2): 551-555. <http://hdl.handle.net/2027.42/24002>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DV0952-1JG/2/a80007709985cbb10b3707920d9b8926en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24002
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6284055&dopt=citationen_US
dc.description.abstractThe recent assertion of [1.] that Fe-EDTA does not catalyze superoxide dismutation is disputed. By directly observing superoxide generated during pulse radiolysis, we have confirmed the results of a previous study ( [2.]) which concluded that Fe-EDTA catalyzed superoxide dismutation. We also demonstrate that the reaction of Fe(II)-EDTA, formed during catalyzed superoxide dismutation, with cytochrome c, the probe molecule in the cytochrome c/xanthine oxidase/xanthine assay system for superoxide dismutase activity, is sufficiently rapid ([12.]) to obscure the weak catalysis of superoxide dismutation by Fe-EDTA.en_US
dc.format.extent392336 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleIron-ethylenediaminetetraacetic acid (EDTA)-catalyzed superoxide dismutation revisited: An explanation of why the dismutase activity of Fe-EDTA cannot be detected in the cytochrome c/xanthine oxidase assay systemen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationotherDivision of Physics, Institute of Cancer Research, Clifton Avenue, Surrey SM2 2PX, United Kingdomen_US
dc.contributor.affiliationotherDivision of Physics, Institute of Cancer Research, Clifton Avenue, Surrey SM2 2PX, United Kingdomen_US
dc.identifier.pmid6284055en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24002/1/0000251.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(82)90115-1en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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