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.

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>

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

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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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)

Publication year

2013

Confidentiality

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

Name of the periodical

Electrophoresis

ISSN

0173-0835

e-ISSN

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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

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