Tyrosine Residues Modifications Studied by MALDI-TOF MS

Result code in 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>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Tyrosine Residues Modifications Studied by MALDI-TOF MS
Original language description
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
Czech name
Studium modifikací tyrosinu pomocí MALDI-TOF MS
Czech description
Studium modifikací tyrosinu pomocí MALDI-TOF MS

Project
<a href="/en/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)