Studium modifikací tyrosinu pomocí MALDI-TOF MS

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012918" target="_blank" >RIV/60461373:22330/04:00012918 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Tyrosine Residues Modifications Studied by MALDI-TOF MS

Popis výsledku v původním jazyce

Tyrosine residue is often a target of biologically interesting posttranslational modifications. Among them, phosphorylation, which plays pivotal roles in regulation of protein activity and thus also in signal transduction pathways, and nitration, which is associated with oxidative stress, are believed to be the most important ones.In the first part of this study we used chemical modification of tyrosine residues of model proteins by tetranitomethane to verify the possibility to detect localization of aromatic groups on the surface of protein globule. The modified tyrosine residues were localized by tryptic cleavage and MALDI-TOF MS. The method for determination of surface tyrosine residues which represent potential targets for posttranslational modifications was developed. Secondly we localized natural occuring posttranslational phosphorylation of plant phospholipase D from Brasica oleracea var capitata. This was performed by comparison of MALDI-TOF MS spectra of tryptic digests of pho

Název v anglickém jazyce

Tyrosine Residues Modifications Studied by MALDI-TOF MS

Popis výsledku anglicky

Tyrosine residue is often a target of biologically interesting posttranslational modifications. Among them, phosphorylation, which plays pivotal roles in regulation of protein activity and thus also in signal transduction pathways, and nitration, which is associated with oxidative stress, are believed to be the most important ones.In the first part of this study we used chemical modification of tyrosine residues of model proteins by tetranitomethane to verify the possibility to detect localization of aromatic groups on the surface of protein globule. The modified tyrosine residues were localized by tryptic cleavage and MALDI-TOF MS. The method for determination of surface tyrosine residues which represent potential targets for posttranslational modifications was developed. Secondly we localized natural occuring posttranslational phosphorylation of plant phospholipase D from Brasica oleracea var capitata. This was performed by comparison of MALDI-TOF MS spectra of tryptic digests of pho

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Studium konformace bílkovin pomocí hmotnostní spektrometrie na principu MALDI-TOF (Matrix Assisted Laser Desorption Ionisation - Time Of Flight)</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

Mass Spectrometry in Systems Biology

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

50

Název nakladatele

neuveden

Místo vydání

Santa Fe - New Mexico - USA

Místo konání akce

Santa Fe - New Mexico - USA

Datum konání akce

14. 2. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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