Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
Апстракт
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.
Извор:
Russian Journal of Physical Chemistry A, 2008, 82, 5, 870-874
DOI: 10.1134/S0036024408050312
ISSN: 0036-0244
WoS: 000255747800031
Scopus: 2-s2.0-43449130920
Колекције
Институција/група
VinčaTY - 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 . .