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dc.contributor.authorAugustyniak, Edyta
dc.contributor.authorAdam, Aisha
dc.contributor.authorWojdyla, Katarzyna
dc.contributor.authorRogowska-Wrzesinska, Adelina
dc.contributor.authorWilletts, Rachel
dc.contributor.authorKorkmaz, Ayhan
dc.contributor.authorAtalay, Mustafa
dc.contributor.authorWeber, Daniela
dc.contributor.authorGrune, Tilman
dc.contributor.authorBorsa, Claudia
dc.contributor.authorGradinaru, Daniela
dc.contributor.authorChand Bollineni, Ravi
dc.contributor.authorFedorova, Maria
dc.contributor.authorGriffiths, Helen R.
dc.date.accessioned2016-06-08T10:36:22Z
dc.date.available2016-06-08T10:36:22Z
dc.date.issued2014-12-24
dc.identifierdoi: 10.1016/j.redox.2014.12.014
dc.identifier.citationAugustyniak, Edyta, Adam, Aisha, Wojdyla, Katarzyna, Rogowska-Wrzesinska, Adelina, Willetts, Rachel, Korkmaz, Ayhan, Atalay, Mustafa, Weber, Daniela, Grune, Tilman, Borsa, Claudia, Gradinaru, Daniela, Chand Bollineni, Ravi, Fedorova, Maria, Griffiths, Helen R. Validation of protein carbonyl measurement: A multi-centre study. Redox Biology Vol.: 4. Elsevier BV 24.12.2014. issn: 2213-2317. doi: 10.1016/j.redox.2014.12.014.fi_FI
dc.identifier.issn2213-2317
dc.identifier.urihttps://erepo.uef.fi/handle/123456789/50
dc.descriptionArticle
dc.description.abstractProtein carbonyls are widely analysed as a measure of protein oxidation. Several different methods exist for their determination. A previous study had described orders of magnitude variance that existed when protein carbonyls were analysed in a single laboratory by ELISA using different commercial kits. We have further explored the potential causes of variance in carbonyl analysis in a ring study. A soluble protein fraction was prepared from rat liver and exposed to 0, 5 and 15 min of UV irradiation. Lyophilised preparations were distributed to six different laboratories that routinely undertook protein carbonyl analysis across Europe. ELISA and Western blotting techniques detected an increase in protein carbonyl formation between 0 and 5 min of UV irradiation irrespective of method used. After irradiation for 15 min, less oxidation was detected by half of the laboratories than after 5 min irradiation. Three of the four ELISA carbonyl results fell within 95% confidence intervals. Likely errors in calculating absolute carbonyl values may be attributed to differences in standardisation. Out of up to 88 proteins identified as containing carbonyl groups after tryptic cleavage of irradiated and control liver proteins, only seven were common in all three liver preparations. Lysine and arginine residues modified by carbonyls are likely to be resistant to tryptic proteolysis. Use of a cocktail of proteases may increase the recovery of oxidised peptides. In conclusion, standardisation is critical for carbonyl analysis and heavily oxidised proteins may not be effectively analysed by any existing technique.fi_FI
dc.language.isoenfi_FI
dc.publisherElsevier BVfi_FI
dc.relation.ispartofseriesRedox Biology
dc.relation.urihttp://dx.doi.org/10.1016/j.redox.2014.12.014
dc.rightsCC BY-NC-ND 4.0 http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectProtein oxidationfi_FI
dc.subjectCarbonyl ELISAfi_FI
dc.subjectOxidised protein Western blotfi_FI
dc.subjectAldehyde reactive probefi_FI
dc.subjectMass spectrometryfi_FI
dc.titleValidation of protein carbonyl measurement: A multi-centrefi_FI
dc.typehttp://purl.org/eprint/type/JournalArticle
dc.description.versionPublisher's pdf
dc.contributor.departmentFaculty of Health Sciences
uef.solecris.id34391206
eprint.statushttp://purl.org/eprint/status/PeerReviewed
dc.type.publicationinfo:eu-repo/semantics/article
dc.rights.accessrights© Clearance Center, Inc
dc.relation.doi10.1016/j.redox.2014.12.014
dc.description.reviewstatushttp://purl.org/eprint/status/PeerReviewed
dc.relation.issn2213-2317
dc.relation.volume4
dc.rights.accesslevelopenAccess


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