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

uri

http://link.springer.com/content/pdf/10.1134/S0036024408050312.pdf

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

This item was submitted on 29. новембар 2023. by [anonymous user] using the form “Рад у часопису” on the site “Радови”: http://gabp-dl.rgf.rs/s/repo