Effects of ex situ chronopotentiometric analysis on stability of bovine serum albumin on mercury electrodes

Časopis: Journal of Electroanalytical Chemistry, 860 (2020) p. 113884
Autoři: Ostatná V., West R.M.
Rok: 2020
ISBN: 1572-6657

Abstrakt

Constant current chronopotentiometric stripping (CPS) allows analysis ofproteins based onmeasured peakH resulting fromcatalytic hydrogen evolution reaction. The technique is label-free and sensitive to the structure and stability ofthe protein adsorbed at the mercury electrode. Comparison ofproteins must be carried out under the same conditions, in- cluding ionic strength, temperature, pH, and accumulation potential and time, as all of these factors can affect the pro- tein 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 sus- ceptibility to electric field-induced denaturation during the subsequent CPS measurement. This destabilization is at- tributed to oxidation of the Hg electrode during disconnection. For this reason, care much be taken when ex situ CPS measurement of protein is performed.

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