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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F11%3A43891979%21RIV12-MSM-22330___
rdf:type
n5:Vysledek skos:Concept
dcterms:description
Plant seed oil bodies, subcellular lipoprotein inclusions providing storage reserves, are composed of a neutral lipid core surrounded by a phospholipid monolayer with several integrated proteins that play a significant role in stabilization of the particles and probably also in lipid mobilization. Oil bodies' proteins are generally very hydrophobic, due to the long uncharged sequences anchoring them into the lipid core, which makes them extremely difficult to handle and to digest successfully. Although oil bodies have been intensively studied during last decades, not all their proteins have been identified yet. To overcome the problems connected with their identification, a method based on SDS-PAGE, in-gel digestion and LC-MS/MS analysis was used. Digestion was carried out with trypsin and chymotrypsin, single or in combination, which increased significantly the number of identified peptides, namely the hydrophobic ones. Thanks to this methodology it was possible to achieve an extensive coverage of proteins studied, to analyze their N-terminal modifications and moreover, to detect four new oil bodies' protein isoforms, which demonstrates the complexity of oil bodies' protein composition. Plant seed oil bodies, subcellular lipoprotein inclusions providing storage reserves, are composed of a neutral lipid core surrounded by a phospholipid monolayer with several integrated proteins that play a significant role in stabilization of the particles and probably also in lipid mobilization. Oil bodies' proteins are generally very hydrophobic, due to the long uncharged sequences anchoring them into the lipid core, which makes them extremely difficult to handle and to digest successfully. Although oil bodies have been intensively studied during last decades, not all their proteins have been identified yet. To overcome the problems connected with their identification, a method based on SDS-PAGE, in-gel digestion and LC-MS/MS analysis was used. Digestion was carried out with trypsin and chymotrypsin, single or in combination, which increased significantly the number of identified peptides, namely the hydrophobic ones. Thanks to this methodology it was possible to achieve an extensive coverage of proteins studied, to analyze their N-terminal modifications and moreover, to detect four new oil bodies' protein isoforms, which demonstrates the complexity of oil bodies' protein composition.
dcterms:title
New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis
skos:prefLabel
New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis
skos:notation
RIV/60461373:22330/11:43891979!RIV12-MSM-22330___
n5:predkladatel
n19:orjk%3A22330
n3:aktivita
n4:Z n4:S n4:P
n3:aktivity
P(LC06034), S, Z(MSM6046137305)
n3:cisloPeriodika
16
n3:dodaniDat
n8:2012
n3:domaciTvurceVysledku
n11:3608905 n11:9046976 n11:1016539 n11:1120530
n3:druhVysledku
n12:J
n3:duvernostUdaju
n18:S
n3:entitaPredkladatele
n21:predkladatel
n3:idSjednocenehoVysledku
215877
n3:idVysledku
RIV/60461373:22330/11:43891979
n3:jazykVysledku
n15:eng
n3:klicovaSlova
N-terminal post-translational modification; Plant proteomics; Oil bodies; LC-MS/MS; Chymotrypsin; Arabidopsis thaliana
n3:klicoveSlovo
n9:LC-MS%2FMS n9:Chymotrypsin n9:Oil%20bodies n9:Arabidopsis%20thaliana n9:N-terminal%20post-translational%20modification n9:Plant%20proteomics
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[0BD9B39CADD2]
n3:nazevZdroje
Proteomics
n3:obor
n16:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
6
n3:projekt
n20:LC06034
n3:rokUplatneniVysledku
n8:2011
n3:svazekPeriodika
11
n3:tvurceVysledku
Chardot, Thierry Purkrtová, Zita Vermachová, Martina Kodíček, Milan Šantrůček, Jiří Jolivet, Pascale
n3:wos
000294463000017
n3:zamer
n10:MSM6046137305
s:issn
1615-9853
s:numberOfPages
5
n6:doi
10.1002/pmic.201000603
n17:organizacniJednotka
22330