0523951 - BFÚ 2021 RIV CH eng J - Článek v odborném periodiku
Ostatná, Veronika - West, R. M.
Effects of ex situ chronopotentiometric analysis on stability of bovine serum albumin on mercury electrodes.
Journal of Electroanalytical Chemistry. Roč. 860, 1.3.2020 (2020), č. článku 113884. ISSN 1572-6657. E-ISSN 1873-2569
Grant CEP: GA ČR(CZ) GA18-18154S
Institucionální podpora: RVO:68081707
Klíčová slova: hydrogen evolution * proteins * catalysis * electrochemistry
Obor OECD: Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Impakt faktor: 4.464, rok: 2020
Způsob publikování: Omezený přístup
https://www.sciencedirect.com/science/article/abs/pii/S1572665720300679?via%3Dihub

Constant current chronopotentiometric stripping (CPS) allows analysis of proteins based on measured peak H resulting from catalytic hydrogen evolution reaction. The technique is label-free and sensitive to the structure and stability of the protein adsorbed at the mercury electrode. Comparison of proteins must be carried out under the same conditions, including ionic strength, temperature, pH, and accumulation potential and time, as all of these factors can affect the protein stability and structure on the electrode surface. Here we show that for bovine serum albumin, uncontrolled disconnection of the cell after accumulation, as is necessary for ex situ CPS measurements, can cause an increased susceptibility to electric field-induced denaturation during the subsequent CPS measurement. This destabilization is attributed to oxidation of the Hg electrode during disconnection. For this reason, care much be taken when ex situ CPS measurement of protein is performed. (C) 2020 Elsevier B.V. All rights reserved.
Trvalý link: http://hdl.handle.net/11104/0308261