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Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent generating oxidase from human neutrophils
dc.contributor.authorGabig, Theodore G.en_US
dc.contributor.authorLefker, Bruce A.en_US
dc.date.accessioned2006-04-07T18:32:00Z
dc.date.available2006-04-07T18:32:00Z
dc.date.issued1984-01-30en_US
dc.identifier.citationGabig, Theodore G., Lefker, Bruce A. (1984/01/30)."Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent generating oxidase from human neutrophils." Biochemical and Biophysical Research Communications 118(2): 430-436. <http://hdl.handle.net/2027.42/24928>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4F031HH-S1/2/7d29ad91157127b926ed1be98b7efb83en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24928
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6704087&dopt=citationen_US
dc.description.abstractThe resolved flavoprotein and cytochrome b559 components of the NADPH dependent generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.en_US
dc.format.extent406096 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCatalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent generating oxidase from human neutrophilsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumAnn Arbor VA Hospital, Ann Arbor, MI, USA; Department of Medicine, University of Michigan School of Medicine, Ann Arbor, MI, USA.en_US
dc.contributor.affiliationumAnn Arbor VA Hospital, Ann Arbor, MI, USA; Department of Medicine, University of Michigan School of Medicine, Ann Arbor, MI, USA.en_US
dc.identifier.pmid6704087en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24928/1/0000355.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(84)91321-4en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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