Native and denatured enzyme enterokinase determined by electrochemical methods

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...

Full description

Saved in:
Bibliographic Details
Published in:Monatshefte für Chemie 2017-03, Vol.148 (3), p.549-553
Main Authors: Janovjáková, Alica, Gál, Miroslav, Krahulec, Ján, Sokolová, Romana, Naumowicz, Monika, Híveš, Ján
Format: Article
Language:English
Subjects:
Analytical Chemistry
Biomolecules
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Inorganic Chemistry
Organic Chemistry
Original Paper
Physical Chemistry
Proteins
Theoretical and Computational Chemistry
Voltammetry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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. Graphical abstract
ISSN:0026-9247
1434-4475
DOI:10.1007/s00706-016-1915-3