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dc.contributor.authorBurniston, Jatin G.
dc.contributor.authorConnolly, Joanne
dc.contributor.authorKainulainen, Heikki
dc.contributor.authorBritton, Steven L.
dc.contributor.authorKoch, Lauren G.
dc.date.accessioned2019-09-30T12:15:33Z
dc.date.available2019-09-30T12:15:33Z
dc.date.issued2014
dc.identifier.citationBurniston, J. G., Connolly, J., Kainulainen, H., Britton, S. L., & Koch, L. G. (2014). Label-free profiling of skeletal muscle using high-definition mass spectrometry. <i>Proteomics</i>, <i>14</i>(20), 2339-2344. <a href="https://doi.org/10.1002/pmic.201400118" target="_blank">https://doi.org/10.1002/pmic.201400118</a>
dc.identifier.otherCONVID_23916251
dc.identifier.otherTUTKAID_63272
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/65684
dc.description.abstractWe report automated and time‐efficient (2 h per sample) profiling of muscle using ultra‐performance LC coupled directly with high‐definition MS (HDMSE). Soluble proteins extracted from rat gastrocnemius (n = 10) were digested with trypsin and analyzed in duplicate using a 90 min RPLC gradient. Protein identification and label‐free quantitation were performed from HDMSE spectra analyzed using Progenesis QI for Proteomics software. In total 1514 proteins were identified. Of these, 811 had at least three unique peptides and were subsequently used to assess the dynamic range and precision of LC‐HDMSE label‐free profiling. Proteins analyzed by LC‐HDMSE encompass the entire complement of glycolytic, β‐oxidation, and tricarboxylic acid enzymes. In addition, numerous components of the electron transport chain and protein kinases involved in skeletal muscle regulation were detected. The dynamic range of protein abundances spanned four orders of magnitude. The correlation between technical replicates of the ten biological samples was R2 = 0.9961 ± 0.0036 (95% CI = 0.9940 – 0.9992) and the technical CV averaged 7.3 ± 6.7% (95% CI = 6.87 – 7.79%). This represents the most sophisticated label‐free profiling of skeletal muscle to date.fi
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherWiley-VCH Verlag
dc.relation.ispartofseriesProteomics
dc.rightsIn Copyright
dc.subject.otheranimal proteomics
dc.subject.otherdata-independent acquisition
dc.subject.otherion mobility
dc.subject.otherLC-MS
dc.titleLabel-free profiling of skeletal muscle using high-definition mass spectrometry
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201909094063
dc.contributor.laitosLiikuntabiologian laitosfi
dc.contributor.laitosDepartment of Biology of Physical Activityen
dc.contributor.oppiaineLiikuntafysiologiafi
dc.contributor.oppiaineExercise Physiologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2019-09-09T12:15:15Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange2339–2344
dc.relation.issn1615-9861
dc.relation.numberinseries20
dc.relation.volume14
dc.type.versionacceptedVersion
dc.rights.copyright© 2014 WILEY‐VCH Verlag GmbH & Co
dc.rights.accesslevelopenAccessfi
dc.format.contentfulltext
dc.rights.urlhttp://rightsstatements.org/page/InC/1.0/?language=en
dc.relation.doi10.1002/pmic.201400118
dc.type.okmA1


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