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Zeitschrift für Naturforschung C

A Journal of Biosciences

Editor-in-Chief: Seibel, Jürgen

Editorial Board: Aigner , Achim / Boland, Wilhelm / Bornscheuer, Uwe / Hoffmann, Klaus

12 Issues per year


IMPACT FACTOR 2017: 0.882
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1865-7125
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Volume 73, Issue 9-10

Issues

Why is the hydrolytic activity of acetylcholinesterase pH dependent? Kinetic study of acetylcholine and acetylthiocholine hydrolysis catalyzed by acetylcholinesterase from electric eel

Alena Komersová
  • Department of Physical Chemistry, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 532 10 Pardubice, Czech Republic
  • Other articles by this author:
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/ Markéta Kovářová
  • Department of Physical Chemistry, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 532 10 Pardubice, Czech Republic
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/ Karel Komers
  • Department of Physical Chemistry, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 532 10 Pardubice, Czech Republic
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/ Václav Lochař
  • Corresponding author
  • Department of Physical Chemistry, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 532 10 Pardubice, Czech Republic, Fax: +420-466-037-068
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/ Alexander Čegan
  • Department of Biological and Biochemical Sciences, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 523 10 Pardubice, Czech Republic
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Published Online: 2018-06-25 | DOI: https://doi.org/10.1515/znc-2017-0134

Abstract

The dependence of the activity of acetylcholinesterase from electric eel at a pH value range of 4.8–9.8 (phosphate buffer), regarding acetylcholine and acetylthiocholine hydrolysis, was determined at 25 °C, ionic strength of 0.11 M, and initial substrate concentration of 4 mM. At a pH range of 4.8–9.8, the dependences A(pH) form a sigmoid increasing curve with the maximum catalytic activity at a pH range 8–9.5. For acetylcholine hydrolysis, the kinetic reason for such an increase in A consists mainly of an increase in the rate constant k2 (Michaelis-Menten) model with increasing pH of the reaction mixture. For acetylthiocholine hydrolysis, the kinetic explication of the determined dependence A(pH) is more complicated.

Keywords: acetylcholinesterase; enzyme activity; kinetics; pH dependence

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About the article

Received: 2017-07-25

Revised: 2018-03-22

Accepted: 2018-04-16

Published Online: 2018-06-25

Published in Print: 2018-09-25


Funding Source: Ministry of Education

Award identifier / Grant number: SGS_2017_007

This work was supported by the Ministry of Education, Youth and Sports of the Czech Republic no. SGS_2017_007.


Conflict of interest statement: The authors report no declarations of interest.


Citation Information: Zeitschrift für Naturforschung C, Volume 73, Issue 9-10, Pages 345–351, ISSN (Online) 1865-7125, ISSN (Print) 0939-5075, DOI: https://doi.org/10.1515/znc-2017-0134.

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