Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/28191
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dc.contributor.authorVollaard, Nielsen_UK
dc.contributor.authorReeder, Brandon Jen_UK
dc.contributor.authorShearman, Jerry Pen_UK
dc.contributor.authorMenu, Patricken_UK
dc.contributor.authorWilson, Michael Ten_UK
dc.contributor.authorCooper, Chris Een_UK
dc.date.accessioned2018-11-09T12:25:17Z-
dc.date.available2018-11-09T12:25:17Z-
dc.date.issued2005-11-01en_UK
dc.identifier.urihttp://hdl.handle.net/1893/28191-
dc.description.abstractFree radical formation in heme proteins is recognised as a factor in mediating the toxicity of peroxides in oxidative stress. As well as initiating free radical damage, heme proteins damage themselves. Under extreme conditions, where oxidative stress and low pH coincide (e.g., myoglobin in the kidney following rhabdomyolysis and hemoglobin in the CSF subsequent to subarachnoid hemorrhage), peroxide can induce covalent heme to protein cross-linking. In this paper we show that, even at neutral pH, the heme in hemoglobin is covalently modified by oxidation. The product, which we term OxHm, is a "green heme" iron chlorin with a distinct optical spectrum. OxHm formation can be quantitatively prevented by reductants of ferryl iron, e.g., ascorbate. We have developed a simple, robust, and reproducible HPLC assay to study the extent of OxHm formation in the red cell in vivo. We show that hemoglobin is oxidatively damaged even in normal blood; approximately 1 in 2000 heme groups exist as OxHm in the steady state. We used a simple model (physical exercise) to demonstrate that OxHm increases significantly during acute oxidative stress. The exercise-induced increase is short-lived, suggesting the existence of an active mechanism for repairing or removing the damaged heme proteins.en_UK
dc.language.isoenen_UK
dc.publisherElsevieren_UK
dc.relationVollaard N, Reeder BJ, Shearman JP, Menu P, Wilson MT & Cooper CE (2005) A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo. Free Radical Biology and Medicine, 39 (9), pp. 1216-1228. https://doi.org/10.1016/j.freeradbiomed.2005.06.012en_UK
dc.rightsThe publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.en_UK
dc.rights.urihttp://www.rioxx.net/licenses/under-embargo-all-rights-reserveden_UK
dc.subjectFree radicalen_UK
dc.subjectHemoglobinen_UK
dc.subjectMyoglobinen_UK
dc.subjectPeroxideen_UK
dc.subjectExerciseen_UK
dc.subjectOxidative stressen_UK
dc.subjectBlood substituteen_UK
dc.subjectOxidative modificationen_UK
dc.subjectAssayen_UK
dc.subjectChlorinen_UK
dc.titleA new sensitive assay reveals that hemoglobin is oxidatively modified in vivoen_UK
dc.typeJournal Articleen_UK
dc.rights.embargodate2999-12-31en_UK
dc.rights.embargoreason[Vollaard_Free_Radical_Biology_and_Medicine_2005.pdf] The publisher does not allow this work to be made publicly available in this Repository therefore there is an embargo on the full text of the work.en_UK
dc.identifier.doi10.1016/j.freeradbiomed.2005.06.012en_UK
dc.identifier.pmid16214037en_UK
dc.citation.jtitleFree Radical Biology and Medicineen_UK
dc.citation.issn0891-5849en_UK
dc.citation.volume39en_UK
dc.citation.issue9en_UK
dc.citation.spage1216en_UK
dc.citation.epage1228en_UK
dc.citation.publicationstatusPublisheden_UK
dc.citation.peerreviewedRefereeden_UK
dc.type.statusVoR - Version of Recorden_UK
dc.author.emailn.vollaard@stir.ac.uken_UK
dc.citation.date10/08/2005en_UK
dc.contributor.affiliationHeriot-Watt Universityen_UK
dc.contributor.affiliationUniversity of Essexen_UK
dc.contributor.affiliationUniversity of Essexen_UK
dc.contributor.affiliationUniversity Henri Poincareen_UK
dc.contributor.affiliationUniversity of Essexen_UK
dc.contributor.affiliationUniversity of Essexen_UK
dc.identifier.isiWOS:000232870700010en_UK
dc.identifier.scopusid2-s2.0-26044483791en_UK
dc.identifier.wtid546259en_UK
dc.contributor.orcid0000-0002-4576-8879en_UK
dc.date.accepted2005-06-21en_UK
dcterms.dateAccepted2005-06-21en_UK
dc.date.filedepositdate2018-11-07en_UK
rioxxterms.apcnot requireden_UK
rioxxterms.typeJournal Article/Reviewen_UK
rioxxterms.versionVoRen_UK
local.rioxx.authorVollaard, Niels|0000-0002-4576-8879en_UK
local.rioxx.authorReeder, Brandon J|en_UK
local.rioxx.authorShearman, Jerry P|en_UK
local.rioxx.authorMenu, Patrick|en_UK
local.rioxx.authorWilson, Michael T|en_UK
local.rioxx.authorCooper, Chris E|en_UK
local.rioxx.projectInternal Project|University of Stirling|https://isni.org/isni/0000000122484331en_UK
local.rioxx.freetoreaddate1970-01-01en_UK
local.rioxx.licencehttp://www.rioxx.net/licenses/under-embargo-all-rights-reserved||en_UK
local.rioxx.filenameVollaard_Free_Radical_Biology_and_Medicine_2005.pdfen_UK
local.rioxx.filecount1en_UK
local.rioxx.source0891-5849en_UK
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