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Statements

Subject Item
n2:RIV%2F68081715%3A_____%2F13%3A00422562%21RIV14-MSM-68081715
rdf:type
skos:Concept n10:Vysledek
dcterms:description
N-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. N-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.
dcterms:title
Optimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study Optimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study
skos:prefLabel
Optimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study Optimization of N-glycopeptides analysis methods and their preliminary application to barley proteins study
skos:notation
RIV/68081715:_____/13:00422562!RIV14-MSM-68081715
n10:predkladatel
n15:ico%3A68081715
n3:aktivita
n18:P n18:I
n3:aktivity
I, P(EE2.3.20.0182), P(GPP503/12/P395)
n3:dodaniDat
n8:2014
n3:domaciTvurceVysledku
n4:5535913 n4:4784111 n4:6775993 n4:6104851
n3:druhVysledku
n20:D
n3:duvernostUdaju
n12:S
n3:entitaPredkladatele
n14:predkladatel
n3:idSjednocenehoVysledku
94481
n3:idVysledku
RIV/68081715:_____/13:00422562
n3:jazykVysledku
n19:eng
n3:klicovaSlova
glycosylation; post-translational modification; barley; N-glycopetptides
n3:klicoveSlovo
n16:barley n16:glycosylation n16:post-translational%20modification n16:N-glycopetptides
n3:kontrolniKodProRIV
[1D2E10FFD311]
n3:mistoKonaniAkce
Brno
n3:mistoVydani
Praha
n3:nazevZdroje
Chemické Listy. Roč. 107, Issue s3.
n3:obor
n11:CB
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
4
n3:projekt
n17:EE2.3.20.0182 n17:GPP503%2F12%2FP395
n3:rokUplatneniVysledku
n8:2013
n3:tvurceVysledku
Benkovská, Dagmar Flodrová, Dana Laštovičková, Markéta Bobálová, Janette
n3:typAkce
n7:WRD
n3:wos
000328730800005
n3:zahajeniAkce
2013-11-12+01:00
s:issn
1213-7103
s:numberOfPages
3
n6:hasPublisher
Česká společnost chemická