"Studium modifikac\u00ED tyrosinu pomoc\u00ED MALDI-TOF MS"@cs . . "1"^^ . "Neuveden" . "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 phosphorylated form"@en . "Novotn\u00E1, Zuzana" . "5"^^ . "Tyrosine Residues Modifications Studied by MALDI-TOF MS" . "Santa Fe - New Mexico - USA" . . "RIV/60461373:22330/04:00012918!RIV/2005/GA0/223305/N" . "Santa Fe - New Mexico - USA" . "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 phosphorylated form" . . "P(GA203/02/0922), Z(MSM 223300006)" . "50" . . "Kadl\u010D\u00EDk, Vojt\u011Bch" . "[FFA7FF23E83C]" . "5"^^ . . . . . . "Tyrosine Residues Modifications Studied by MALDI-TOF MS"@en . . "Tyrosine Residues Modifications Studied by MALDI-TOF MS" . . "22330" . "Studium modifikac\u00ED tyrosinu pomoc\u00ED MALDI-TOF MS"@cs . . . . "Kod\u00ED\u010Dek, Milan" . "RIV/60461373:22330/04:00012918" . "591123" . . "Hynek, Radovan" . "Studium modifikac\u00ED tyrosinu pomoc\u00ED MALDI-TOF MS"@cs . . . . "\u0160antr\u016F\u010Dek, Ji\u0159\u00ED" . "tyrosine phosphorylation"@en . "Tyrosine Residues Modifications Studied by MALDI-TOF MS"@en . "2004-02-14+01:00"^^ . . "Mass Spectrometry in Systems Biology" . .