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Analysis of the glycosylation pattern of plant copper amine oxidases by MALDI-TOF/TOF mass spectrometry coupled to a manual chromatographic separation of glycans and glycopeptides.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33147871" target="_blank" >RIV/61989592:15310/13:33147871 - isvavai.cz</a>

  • Result on the web

    <a href="http://onlinelibrary.wiley.com/doi/10.1002/elps.201200622/full" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/elps.201200622/full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/elps.201200622" target="_blank" >10.1002/elps.201200622</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Analysis of the glycosylation pattern of plant copper amine oxidases by MALDI-TOF/TOF mass spectrometry coupled to a manual chromatographic separation of glycans and glycopeptides.

  • Original language description

    The N-glycosylation in pea seedling amine oxidase and lentil seedling amine oxidase was analyzed in the present work. For that purpose, the enzymes were purified as native proteins from their natural sources. An enzymatic deglycosylation of pea seedlingamine oxidase by endoglycosidase H under denaturing conditions combined with its proteolytic digestion by trypsin was carried out in order to analyze both N-glycans and "trimmed" N-glycopeptides with a residual N-acetylglucosamine attached at the originally occupied N-glycosylation sites. The released N-glycans were subjected to amanual chromatographic purification followed by MALDI-TOF/TOF MS. MS and MS/MS analyses were also performed directly on peptides and N-glycopeptides generated by proteolytic digestion of the studied enzymes. Sequencing of glycopeptides by MALDI-TOF/TOF MS/MS after their separation on a RP using a microgradient chromatographic device clearly demonstrated binding of paucimannose and hybrid N-glycan structures at

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Electrophoresis

  • ISSN

    0173-0835

  • e-ISSN

  • Volume of the periodical

    34

  • Issue of the periodical within the volume

    16

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    11

  • Pages from-to

    2357-2367

  • UT code for WoS article

    000327665500012

  • EID of the result in the Scopus database