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dc.date.accessioned2020-05-29T18:45:54Z
dc.date.available2020-05-29T18:45:54Z
dc.date.created2019-03-28T12:09:42Z
dc.date.issued2019
dc.identifier.citationSkjærvø, Øystein Trimpin, Sarah Halvorsen, Trine Grønhaug . Matrix assisted ionization mass spectrometry in targeted protein analysis – an initial evaluation. Rapid Communications in Mass Spectrometry. 2019
dc.identifier.urihttp://hdl.handle.net/10852/76451
dc.description.abstractRationale Matrix‐assisted ionization (MAI) is a relatively new ionization technique for analysis by mass spectrometry (MS). The technique is simple and has been shown to be less influenced by matrix effects than e.g. electrospray ionization (ESI). These features are of interest in the targeted analysis of proteins from biological samples. Methods Targeted protein determination by MAI‐MS was evaluated using a triple quadrupole mass analyzer equipped with a stripped nanoESI source in selected reaction monitoring (SRM) mode. The proteins were analyzed using the bottom‐up approach with stable isotopic labeled peptides as internal standards (IS). The MAI matrix was 3‐nitrobenzonitrile dissolved in acetonitrile. Aqueous sample and matrix solution were mixed in a 1:3 volume ratio. One microlitre of the dried matrix/analyte sample was introduced into the inlet of the mass spectrometer where ionization commences. Results SRM settings established for ESI‐SRM‐MS of the peptides here investigated were applicable in MAI‐SRM‐MS for all evaluated peptides except one that is poorly soluble in water. Addition of IS provided efficient correction at most levels (relative standard deviation (RSD) ≤28% (except lowest digest level), r2 ≥ 0.995). This was also true for the more complex biological matrices, diluted urine (1:1; RSD = 20% a synthetic peptide, NLLGLIEAK) and diluted digested serum (1:100; RSD = 7% digested cytochrome C). Biological matrix influenced the signal intensity unless sufficiently diluted. Conclusions The results demonstrate that MAI‐SRM‐MS has promising potential in targeted protein determination by the bottom‐up approach because of its simplicity, ease of use, and speed. However, more data is needed to confirm the results prior to application in a clinical setting.en_US
dc.languageEN
dc.titleMatrix assisted ionization mass spectrometry in targeted protein analysis – an initial evaluationen_US
dc.typeJournal articleen_US
dc.creator.authorSkjærvø, Øystein
dc.creator.authorTrimpin, Sarah
dc.creator.authorHalvorsen, Trine Grønhaug
cristin.unitcode185,15,23,20
cristin.unitnameSeksjon for farmasøytisk kjemi
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode1
dc.identifier.cristin1688512
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Rapid Communications in Mass Spectrometry&rft.volume=&rft.spage=&rft.date=2019
dc.identifier.jtitleRapid Communications in Mass Spectrometry
dc.identifier.doihttps://doi.org/10.1002/rcm.8437
dc.identifier.urnURN:NBN:no-79528
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn0951-4198
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/76451/2/Post%2Bprint%2Bversion.pdf
dc.type.versionAcceptedVersion
cristin.articleidrcm.8437


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