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.

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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.

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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.

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Electrophoresis

ISSN

0173-0835

e-ISSN

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Svazek periodika

34

Číslo periodika v rámci svazku

16

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

2357-2367

Kód UT WoS článku

000327665500012

EID výsledku v databázi Scopus

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