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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F18%3A39912589" target="_blank" >RIV/00216275:25310/18:39912589 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1515/znc-2017-0134" target="_blank" >http://dx.doi.org/10.1515/znc-2017-0134</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1515/znc-2017-0134" target="_blank" >10.1515/znc-2017-0134</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 degrees 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 k(2) (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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 degrees 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 k(2) (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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Zeitschrift für Naturforschung C = A Journal of Biosciences

ISSN

0939-5075

e-ISSN

—

Svazek periodika

73

Číslo periodika v rámci svazku

9-10

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

7

Strana od-do

345-351

Kód UT WoS článku

000444081500003

EID výsledku v databázi Scopus

2-s2.0-85049510320