Number of the records: 1  

Optimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study

  1. 1.
    SYSNO ASEP0422562
    Document TypeC - Proceedings Paper (int. conf.)
    R&D Document TypeConference Paper
    TitleOptimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study
    Author(s) Benkovská, Dagmar (UIACH-O)
    Flodrová, Dana (UIACH-O)
    Bobálová, Janette (UIACH-O) RID, ORCID
    Laštovičková, Markéta (UIACH-O) RID, ORCID
    Number of authors4
    Source TitleChemické Listy. Roč. 107, Issue s3.. - Praha : Česká společnost chemická, 2013 - ISSN 0009-2770
    Pagess. 296-298
    Number of pages3 s.
    Publication formOnline - E
    ActionCECE Junior 2013
    Event date12.11.2013-13.11.2013
    VEvent locationBrno
    CountryCZ - Czech Republic
    Event typeWRD
    Languageeng - English
    CountryCZ - Czech Republic
    Keywordsglycosylation ; post-translational modification ; barley ; N-glycopetptides
    Subject RIVCB - Analytical Chemistry, Separation
    R&D ProjectsEE2.3.20.0182 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    GPP503/12/P395 GA ČR - Czech Science Foundation (CSF)
    Institutional supportUIACH-O - RVO:68081715
    UT WOS000328730800005
    AnnotationN-glycosylation is the most frequently studied plant protein post-translational modification. The analysis of Nglycopeptides after protein proteolytic digestion offers information about the structure of both oligosaccharide and peptide moiety. However, this method has so far been less commonly used. Since glycopeptides hardly ionize during MS analysis in the presence of non-glycosylated peptides, they need to be separated from the complex peptide mixture. In this study, the glycopeptides enrichment, purification and analysis methods were successfully optimized on two standard N-glycoproteins. Concanavalin A (ConA) lectin tips were used for glycopeptide capturing, and obtained fractions were purified on carbon tips and analyzed using MALDI-TOF mass spectrometry. The differences in the CID fragmentation of certain types of glycopeptides were found. This technique was then applied to glycopeptide analysis of barley grain and malt proteins. Several barley glycopeptides were found, however, their identification was very difficult. More proteins separation techniques will be required before this enrichment procedure in further studies.
    WorkplaceInstitute of Analytical Chemistry
    ContactIveta Drobníková, drobnikova@iach.cz, Tel.: 532 290 234
    Year of Publishing2014
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.