Kinetika hydrolýzy acetylthiocholinu a acetylcholinu pomocí cholinesteráz

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F05%3A00002848" target="_blank" >RIV/00216275:25310/05:00002848 - 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

Kinetics of Hydrolysis of Acetylthiocholine and Acetylcholine by Cholinesterases.

Popis výsledku v původním jazyce

Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied. ATCH is used for testing of enzymatic hydrolysis of ACH in vitro, because mechanism of ATCH hydrolysisis qualitatively similar to ACH and its reaction course can be quantitatively on-line measured by two independent methods: spectrophotometrical (determination of thiocholine - product of ATCH hydrolysis - using Ellman´s method) and electrochemical (determination of acetic acid - product of ATCH hydrolysis - by pH-stat method). All tested hydrolyses correspond to the Michaelis-Menten´s equation with the second irreversible step up to the total exhaustion of the substrate. The correlations were made by means of differential and integral kinetic equations describing Michaelis-Menten model. The optimal values of Michaelis constant (KM), maximum velocity (Vm), kinetic constants of single reaction steps and absolute concentration of the used

Název v anglickém jazyce

Kinetics of Hydrolysis of Acetylthiocholine and Acetylcholine by Cholinesterases.

Popis výsledku anglicky

Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied. ATCH is used for testing of enzymatic hydrolysis of ACH in vitro, because mechanism of ATCH hydrolysisis qualitatively similar to ACH and its reaction course can be quantitatively on-line measured by two independent methods: spectrophotometrical (determination of thiocholine - product of ATCH hydrolysis - using Ellman´s method) and electrochemical (determination of acetic acid - product of ATCH hydrolysis - by pH-stat method). All tested hydrolyses correspond to the Michaelis-Menten´s equation with the second irreversible step up to the total exhaustion of the substrate. The correlations were made by means of differential and integral kinetic equations describing Michaelis-Menten model. The optimal values of Michaelis constant (KM), maximum velocity (Vm), kinetic constants of single reaction steps and absolute concentration of the used

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

2005

Kód důvěrnosti údajů

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

Název periodika

Chemico-Biological Interactions

ISSN

0009-2797

e-ISSN

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Svazek periodika

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Číslo periodika v rámci svazku

157-158

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

2

Strana od-do

387-388

Kód UT WoS článku

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EID výsledku v databázi Scopus

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