Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12323/4746
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dc.contributor.authorChapman, Anna L. P.-
dc.contributor.authorMocatta, Tessa J.-
dc.contributor.authorShiva, Sruti-
dc.contributor.authorSeidel, Antonia-
dc.contributor.authorChen, Brian-
dc.contributor.authorKhalilova, Irada-
dc.contributor.authorPaumann-Page, Martina E.-
dc.contributor.authorJameson, Guy N. L.-
dc.contributor.authorWinterbourn, Christine C.-
dc.contributor.authorKettle, Anthony J.-
dc.date.accessioned2020-09-18T06:22:01Z-
dc.date.available2020-09-18T06:22:01Z-
dc.date.issued2013-03-
dc.identifier.citationJournal of biological chemistryen_US
dc.identifier.urihttp://hdl.handle.net/20.500.12323/4746-
dc.description.abstractMyeloperoxidase is a neutrophil enzyme that promotes oxidative stress in numerous inflammatory pathologies. It uses hydrogen peroxide to catalyze the production of strong oxidants including chlorine bleach and free radicals. A physiological defense against the inappropriate action of this enzyme has yet to be identified. We found that myeloperoxidase oxidized 75% of the ascorbate in plasma from ceruloplasmin knock-out mice, but there was no significant loss in plasma from wild type animals. When myeloperoxidase was added to human plasma it became bound to other proteins and was reversibly inhibited. Ceruloplasmin was the predominant protein associated with myeloperoxidase. When the purified proteins were mixed, they became strongly but reversibly associated. Ceruloplasmin was a potent inhibitor of purified myeloperoxidase, inhibiting production of hypochlorous acid by 50% at 25 nM.en_US
dc.language.isoenen_US
dc.publisherThe American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.relation.ispartofseriesVol. 288;Issue 9-
dc.titleCeruloplasmin is an endogenous inhibitor of myeloperoxidaseen_US
dc.typeArticleen_US
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