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Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation
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SYSNO ASEP 0502601 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation Author(s) Ostatná, Veronika (BFU-R) RID, ORCID
Kasalová, Veronika (BFU-R) ORCID
Kmetova, K. (CZ)
Šedo, O. (CZ)Number of authors 4 Source Title Journal of Electroanalytical Chemistry. - : Elsevier - ISSN 1572-6657
Roč. 821, JUL 15 2018 (2018), s. 97-103Number of pages 6 s. Publication form Print - P Language eng - English Country CH - Switzerland Keywords constant-current chronopotentiometry ; resolution nmr-spectroscopy ; c-terminal domain ; lysine acetylation Subject RIV CG - Electrochemistry OECD category Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis) R&D Projects GA13-00956S GA ČR - Czech Science Foundation (CSF) Institutional support BFU-R - RVO:68081707 UT WOS 000437818600016 DOI 10.1016/j.jelechem.2017.11.044 Annotation Post-translational modifications play the crucial role in biological systems and the identification of novel post translational modifications and study of their role are gaining much attention in proteomics research. For the first time, we compared methylated and acetylated bovine serum albumin to its native and denatured form using constant current chronopotentiometric stripping analysis, phase sensitive alternating current voltammetry and matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). Our results showed that acetylation of bovine serum albumin resulted in decrease of chronopotentiometric peak H due to modification of electroactive residues, while predominantly non-electroactive residues were modified by methylation of serum albumin. Nevertheless, both modifications altered adsorption of protein at surface and therein influenced chronopotentiometric peak H. MALDI-TOF MS analysis confirmed modifications of serum albumin and was in good agreement with electrochemical results. The present results show the capability of label- and reagent-free electrochemical methods to detect post-translational modifications in proteins. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2019
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