Počet záznamů: 1  

Native and denatured enzyme enterokinase determined by electrochemical methods

  1. 1.
    0473185 - ÚFCH JH 2018 RIV AT eng J - Článek v odborném periodiku
    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
    Institucionální podpora: RVO:61388955
    Klíčová slova: enterokinase * proteins conformation * chronopotentiometry
    Obor OECD: Physical chemistry
    Impakt faktor: 1.285, rok: 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.
    Trvalý link: http://hdl.handle.net/11104/0270346

     
    Název souboruStaženoVelikostKomentářVerzePřístup
    0473185.pdf0500.2 KBVydavatelský postprintvyžádat
     
Počet záznamů: 1  

  Tyto stránky využívají soubory cookies, které usnadňují jejich prohlížení. Další informace o tom jak používáme cookies.