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dc.contributor.authorVehniäinen, Eeva-Riikka
dc.contributor.authorSchultz, Eija
dc.contributor.authorLehtivuori, Heli
dc.contributor.authorIhalainen, Janne
dc.contributor.authorOikari, Aimo
dc.date.accessioned2016-08-10T13:41:02Z
dc.date.available2016-08-10T13:41:02Z
dc.date.issued2012
dc.identifier.citationVehniäinen, E.-R., Schultz, E., Lehtivuori, H., Ihalainen, J., & Oikari, A. (2012). More accuracy to the EROD measurements-The resorufin fluorescence differs between species and individuals. <i>Aquatic Toxicology</i>, <i>116–117</i>(15 July 2012), 102-108. <a href="https://doi.org/10.1016/j.aquatox.2012.03.007" target="_blank">https://doi.org/10.1016/j.aquatox.2012.03.007</a>
dc.identifier.otherCONVID_21502400
dc.identifier.otherTUTKAID_51103
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/50924
dc.description.abstractEthoxyresorufin-O-deethylase (EROD) activity is a biomarker of exposure to planar aromatic hydrocarbons, and it is often measured from the S9 fraction. The effect of the liver S9 fraction of seven boreal freshwater fish species on the fluorescence of resorufin was studied. The S9 fractions diminished resorufin fluorescence by 40–80%, and there were large differences between species. Thus, using a resorufin standard curve without the S9 fraction leads to a large underestimation of the EROD activity. Therefore a microwell plate EROD method was developed that takes into account the effect of each sample on resorufin fluorescence. At least two mechanisms were involved in the decrease of the fluorescence: opaqueness of the sample, and enzymes (DT-diaphorase and plausibly NADPH-CYP450 oxidoreductase) that reduce resorufin to a non-fluorescent form.
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofseriesAquatic Toxicology
dc.relation.urihttp://www.sciencedirect.com/science/article/pii/S0166445X12001063
dc.subject.otherEROD activity
dc.subject.otherResorufin
dc.subject.otherEthoxyresorufin-O-deethylase
dc.subject.otherS9 fraction
dc.titleMore accuracy to the EROD measurements-The resorufin fluorescence differs between species and individuals
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201206071816
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineYmpäristötiedefi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineEnvironmental Scienceen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2012-06-07T03:30:05Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.format.pagerange102-108
dc.relation.issn0166-445X
dc.relation.numberinseries15 July 2012
dc.relation.volume116–117
dc.type.versionacceptedVersion
dc.rights.copyright© Elsevier. This is a final draft version of an article whose final and definitive version has been published by Elsevier.
dc.rights.accesslevelopenAccessfi
dc.subject.ysofluoresenssi
jyx.subject.urihttp://www.yso.fi/onto/yso/p3265
dc.relation.doi10.1016/j.aquatox.2012.03.007


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