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  • Halim, AdnanGothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine (author)

Assignment of Saccharide Identities through Analysis of Oxonium Ion Fragmentation Profiles in LC-MS/MS of Glycopeptides.

  • Article/chapterEnglish2014

Publisher, publication year, extent ...

  • 2014-11-17
  • American Chemical Society (ACS),2014

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/209740
  • https://gup.ub.gu.se/publication/209740URI
  • https://doi.org/10.1021/pr500898rDOI
  • http://kipublications.ki.se/Default.aspx?queryparsed=id:130283080URI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Protein glycosylation plays critical roles in the regulation of diverse biological processes, and determination of glycan structure-function relationships is important to better understand these events. However, characterization of glycan and glycopeptide structural isomers remains challenging and often relies on biosynthetic pathways being conserved. In glycoproteomic analysis with liquid chromatography-tandem mass spectrometry (LC-MS/MS) using collision-induced dissociation (CID), saccharide oxonium ions containing N-acetylhexosamine (HexNAc) residues are prominent. Through analysis of beam-type CID spectra and ion trap CID spectra of synthetic and natively derived N- and O-glycopeptides, we found that the fragmentation patterns of oxonium ions characteristically differ between glycopeptides terminally substituted with GalNAcα1-O-, GlcNAcβ1-O-, Galβ3GalNAcα1-O-, Galβ4GlcNAcβ-O-, and Galβ3GlcNAcβ-O- structures. The difference in the oxonium ion fragmentation profiles of such glycopeptides may thus be used to distinguish among these glycan structures and could be of importance in LC-MS/MS-based glycoproteomic studies.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Westerlind, Ulrika (author)
  • Pett, Christian (author)
  • Schorlemer, Manuel (author)
  • Rüetschi, Ulla,1962Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine(Swepub:gu)xrueul (author)
  • Brinkmalm, GunnarGothenburg University,Göteborgs universitet,Institutionen för neurovetenskap och fysiologi, sektionen för psykiatri och neurokemi,Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry(Swepub:gu)xbrigu (author)
  • Sihlbom, Carina,1973Gothenburg University,Göteborgs universitet,Core Facilities, Proteomics,Core Facilities, Proteomics(Swepub:gu)xsihca (author)
  • Lengqvist, JohanKarolinska Institutet,Gothenburg University,Göteborgs universitet,Core Facilities, Proteomics,Core Facilities, Proteomics (author)
  • Larson, Göran,1953Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine(Swepub:gu)xlarsg (author)
  • Nilsson, Jonas,1970Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine(Swepub:gu)xnjoni (author)
  • Göteborgs universitetInstitutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin (creator_code:org_t)

Related titles

  • In:Journal of proteome research: American Chemical Society (ACS)13:12, s. 6024-321535-39071535-3893

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