Use of recombinant iron-superoxide dismutase as a marker of nitrative stress

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dc.contributor.authorLarrainzar Rodríguez, Estíbaliz
dc.contributor.authorUrarte Rodríguez, Estíbaliz
dc.contributor.authorAuzmendi, Iñigo
dc.contributor.authorAriz Arnedo, Idoia
dc.contributor.authorArrese-Igor Sánchez, César
dc.contributor.authorGonzález García, Esther
dc.contributor.authorMorán Juez, José Fernando
dc.contributor.departmentCiencias del Medio Naturales_ES
dc.contributor.departmentNatura Ingurunearen Zientziakeu
dc.contributor.departmentIdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes_ES
dc.contributor.funderGobierno de Navarra / Nafarroako Gobernua, 57/2007
dc.date.accessioned2025-01-30T09:43:45Z
dc.date.available2025-01-30T09:43:45Z
dc.date.issued2008-04-20
dc.date.updated2025-01-30T09:26:43Z
dc.description.abstractSuperoxide dismutases (SODs; EC 1.15.1.1) are a group of metalloenzymes which are essential to protect cells under aerobic conditions. In biological systems, it has been reported that SODs and other proteins are susceptible to be attacked by peroxynitrite (ONOO-) which can be originated from the reaction of nitric oxide with superoxide radical. ONOO- is a strong oxidant molecule capable of nitrating peptides and proteins at the phenyl side chain of the tyrosine residues. In the present work, bovine serum albumin (BSA) and recombinant iron¿superoxide dismutase from the plant cowpea (Vu_FeSOD) are used as target molecules to estimate ONOO- production. The method employs the compound SIN-1, which simultaneously generates -NO and O2- in aerobic aqueous solutions. First, assay conditions were optimized incubating BSA with different concentrations of SIN-1, and at a later stage, the effect on the tyrosine nitration and catalytic activity of Vu_FeSOD was examined by in-gel activity and spectrophotometric assays. Both BSA and Vu_FeSOD are nitrated in a dose-dependent manner, and, at least in BSA nitration, the reaction seems to be metal catalyzed.en
dc.description.sponsorshipThis work was supported by grant from the Government of Navarre, Spain (Res. 57/2007), and from DGI-MEC, Spain (grant AGL 2007-64432/AGR).
dc.format.mimetypeapplication/pdfen
dc.identifier.citationLarrainzar, E., Urarte, E., Auzmendi, I., Ariz, I., Arrese-Igor, C., González, E.M., Morán, J.F. (2008) Use of recombinant iron-superoxide dismutase as a marker of nitrative stress. Methods in enzymology, 437, 605-618. https://doi.org/10.1016/S0076-6879(07)37031-6
dc.identifier.doi10.1016/S0076-6879(07)37031-6
dc.identifier.issn0076-6879
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/53174
dc.language.isoeng
dc.publisherElservier
dc.relation.ispartofMethods in enzymology, 437(2008), 605-618
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//AGL2007-64432%2FAGR/
dc.relation.publisherversionhttps://doi.org/10.1016/S0076-6879(07)37031-6
dc.rights© 2008 Elsevier Inc. This manuscript version is made available under the CC-BY-NC-ND 4.0
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectSuperoxide dismutaseen
dc.subjectPeroxynitriteen
dc.subjectTyrosine nitrationen
dc.subjectBovine serum albumin (BSA)en
dc.titleUse of recombinant iron-superoxide dismutase as a marker of nitrative stressen
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/acceptedVersion
dspace.entity.typePublication
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