Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

Објеката

Тип
Рад у часопису
Верзија рада
објављена верзија
Језик
енглески
Креатор
V. M. Pavelkić, K. S. Krinulović, J. Z. Savić, M. A. Ilić
Извор
Russian Journal of Physical Chemistry A
Издавач
Pleiades Publishing Ltd
Датум издавања
2008
Сажетак
The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high- and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × 10–9 and 1.48 × 10–5 M for the high- and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × 10–9 and 1.38 × 10–6 M. The Cornish–Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites.

том
82
Број
5
почетак странице
870
крај странице
874
doi
10.1134/S0036024408050312
issn
0036-0244
Subject
Малатион, инхибиција, хумана плазма холинестераза, метода флуоресцентне спектроскопије
Malathion, inhibition, human plasma cholinesterase, fluorescence spectroscopy method
Шира категорија рада
M20
Ужа категорија рада
М23
Права
Отворени приступ
Лиценца
All rights reserved
Формат
.pdf
Скупови објеката
Марија Илић
Radovi istraživača
Медија
s0036024408050312.pdf

V. M. Pavelkić, K. S. Krinulović, J. Z. Savić, M. A. Ilić. "Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method" in Russian Journal of Physical Chemistry A, Pleiades Publishing Ltd (2008). https://doi.org/10.1134/S0036024408050312

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