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Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F18%3A00502601" target="_blank" >RIV/68081707:_____/18:00502601 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14740/18:00106758

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.jelechem.2017.11.044" target="_blank" >http://dx.doi.org/10.1016/j.jelechem.2017.11.044</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.jelechem.2017.11.044" target="_blank" >10.1016/j.jelechem.2017.11.044</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Electroanalytical Chemistry

  • ISSN

    1572-6657

  • e-ISSN

  • Volume of the periodical

    821

  • Issue of the periodical within the volume

    JUL 15 2018

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    6

  • Pages from-to

    97-103

  • UT code for WoS article

    000437818600016

  • EID of the result in the Scopus database