Ilic, M. A.

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  • Ilic, M. A. (1)
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Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

Pavelkić, Vesna M.; Krinulović, Katarina; Savić, Jasmina; Ilic, M. A.

(2008)

TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Krinulović, Katarina
AU  - Savić, Jasmina
AU  - Ilic, M. A.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3444
AB  - 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 IC (50) values as calculated from the experimental inhibition curves were 1.33 x 10(-9) and 1.48 x 10(-5) M for the high-and low-affinity binding sites, respectively; Hills analysis gave 1.29 x 10(-9) and 1.38 x 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.
T2  - Russian Journal of Physical Chemistry A
T1  - Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
VL  - 82
IS  - 5
SP  - 870
EP  - 874
DO  - 10.1134/S0036024408050312
ER  - 
@article{
author = "Pavelkić, Vesna M. and Krinulović, Katarina and Savić, Jasmina and Ilic, M. A.",
year = "2008",
abstract = "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 IC (50) values as calculated from the experimental inhibition curves were 1.33 x 10(-9) and 1.48 x 10(-5) M for the high-and low-affinity binding sites, respectively; Hills analysis gave 1.29 x 10(-9) and 1.38 x 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.",
journal = "Russian Journal of Physical Chemistry A",
title = "Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method",
volume = "82",
number = "5",
pages = "870-874",
doi = "10.1134/S0036024408050312"
}
Pavelkić, V. M., Krinulović, K., Savić, J.,& Ilic, M. A.. (2008). Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method. in Russian Journal of Physical Chemistry A, 82(5), 870-874.
https://doi.org/10.1134/S0036024408050312
Pavelkić VM, Krinulović K, Savić J, Ilic MA. Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method. in Russian Journal of Physical Chemistry A. 2008;82(5):870-874.
doi:10.1134/S0036024408050312 .
Pavelkić, Vesna M., Krinulović, Katarina, Savić, Jasmina, Ilic, M. A., "Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method" in Russian Journal of Physical Chemistry A, 82, no. 5 (2008):870-874,
https://doi.org/10.1134/S0036024408050312 . .
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