Abstract
The aim of this work is to detect and distinguish native and denatured form of enzyme enteropeptidase. Cyclic voltammetry is usually the method of choice to be used in experiments with biomolecules or unknown chemical species. However, only hardly detectable differences between native and denatured form of enzyme enterokinase were observed using cyclic voltammetry. Therefore, chronopotentiometric stripping analysis was used for the characterization of protein conformation. Significant differences between the heights of peak H of native and denatured form of enterokinase were observed. Our experiments have proved that constant current chronopotentiometric peak H at mercury electrode is sensitive tool for the characterization of changes in protein conformation.
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Acknowledgements
This research was supported by the Slovak Research and Development Agency under the contract No. APVV-0119-12. This publication is also the result of the project implementation: Centre for materials, layers and systems for applications and chemical processes under extreme conditions-Stage II, ITMS No. 26240120021 supported by the Research and Development Operational Programme funded by the ERDF.
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Janovjáková, A., Gál, M., Krahulec, J. et al. Native and denatured enzyme enterokinase determined by electrochemical methods. Monatsh Chem 148, 549–553 (2017). https://doi.org/10.1007/s00706-016-1915-3
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DOI: https://doi.org/10.1007/s00706-016-1915-3