Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Electroanalytical Chemistry |
| MU Faculty or unit | |
| Citation | |
| Doi | http://dx.doi.org/10.1016/j.jelechem.2017.11.044 |
| Keywords | Bovine serum albumin; Protein acetylation; Protein methylation; Electroactive residues; Catalytic hydrogen evolution reaction; Mercury electrode |
| 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. |
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