Native and denatured enzyme enterokinase determined by electrochemical methods

0473185 - ÚFCH JH 2018 RIV AT eng J - Journal Article
Janovjáková, A. - Gál, M. - Krahulec, J. - Sokolová, Romana - Naumowicz, M. - Híveš, J.
Native and denatured enzyme enterokinase determined by electrochemical methods.
Monatshefte fur Chemie. Roč. 148, č. 3 (2017), s. 549-553. ISSN 0026-9247. E-ISSN 1434-4475
Institutional support: RVO:61388955
Keywords : enterokinase * proteins conformation * chronopotentiometry
OECD category: Physical chemistry
Impact factor: 1.285, year: 2017

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.
Permanent Link: http://hdl.handle.net/11104/0270346