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Constant Current Chronopotentiometry and Voltammetry of Native and Denatured Serum Albumin at Mercury and Carbon Electrodes |
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| Authors: | Veronika Ostatná Filiz Kuralay Libuše Trnková Emil Paleček |
| Institution: | 1. Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i. Královopolská 135, 612?65 Brno, Czech Republic;2. Hacettepe University, Faculty of Science, Department of Chemistry, 06532, Beytepe, Ankara, Turkey;3. Department of Chemistry, Faculty of Science, Masaryk University, Kotlá?ská 2, CZ‐611 37 Brno, Czech Republic |
| Abstract: | Constant current chronopotentiometric peak H at mercury electrodes was recently shown as a sensitive tool for global and local changes in protein conformation 1]. Large differences between the heights of peak H of native (hBSAnat) and denatured BSA (hBSAden) were observed. The ratio hBSAden/hBSAnat increased with more negative stripping current suggesting that the rate of potential change is important for discrimination between native and denatured BSA. Voltammetric peaks of BSA were less well developed and BSAden/BSAnat was much smaller. It was not possible to discriminate BSAden and BSAnat using carbon electrodes. |
| Keywords: | Albumin Chronopotentiometry Protein conformation |