Inhibition of acetylcholinesterase by 14 achiral and five chiral imidazole derivates

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F10%3A39881510" target="_blank" >RIV/00216275:25310/10:39881510 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Inhibition of acetylcholinesterase by 14 achiral and five chiral imidazole derivates

Popis výsledku v původním jazyce

Homological series of 14 nonchiral derivates and series of 5 chiral derivates of imidazole were tested in vitro as inhibitors of hydrolysis of acetylcholine using enzyme preparation of acetylcholine esterase from electric eel. The batch stirred reactor at 25°C, pH 8 (phosphate buffer), ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U ml-1 of the reaction mixture were used. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by an original HPLC method. For all used inhibitors, these time dependences conform with the probability of more than 90 % to the model of competitive irreversible inhibition. All kinetic constants including k3 defining the rate of inhibition (0.71- 5.3 M-1 s-1) and qualified estimation of the absolute acetylcholine esterase concentration in the reaction mixture (40 - 110 nM) were determined.

Název v anglickém jazyce

Inhibition of acetylcholinesterase by 14 achiral and five chiral imidazole derivates

Popis výsledku anglicky

Homological series of 14 nonchiral derivates and series of 5 chiral derivates of imidazole were tested in vitro as inhibitors of hydrolysis of acetylcholine using enzyme preparation of acetylcholine esterase from electric eel. The batch stirred reactor at 25°C, pH 8 (phosphate buffer), ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U ml-1 of the reaction mixture were used. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by an original HPLC method. For all used inhibitors, these time dependences conform with the probability of more than 90 % to the model of competitive irreversible inhibition. All kinetic constants including k3 defining the rate of inhibition (0.71- 5.3 M-1 s-1) and qualified estimation of the absolute acetylcholine esterase concentration in the reaction mixture (40 - 110 nM) were determined.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Bioresource Technology

ISSN

0960-8524

e-ISSN

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Svazek periodika

101

Číslo periodika v rámci svazku

15

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

3

Strana od-do

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Kód UT WoS článku

000278035900080

EID výsledku v databázi Scopus

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