Journal archive > 2011 > N 2 March-April

PECULIARITIES OF THE INFLUENCE OF СETYLTRIMETHYLAMMONIUM
ON THE HUMAN BLOOD CHOLINESTERASES ACTIVITY

L. P. Kuznetsova, V. A. Samokish, E. E. Sochilina

Sechenov Institute of Evolutionary Physiology and Biochemistry,
Russian Academy of Sciences, St. Petersburg, Russia;
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The influence of cationic detergent cetyltrimethylammonium on the human blood cholineste­rases activity (erythrocyte acetylcholinesterase and plasma butyrylcholinesterase) in reactions of hyd­rolysis of ?-thionaphthylacetat and acetylthio­choline is studied. It is shown, that cetyltrimethylammonium is reversible effectоr for both cholineste­rases. This compound competitively inhibited enzymatic hydrolysis of acetylthiocholine by both cholinestera­ses, and in the reactions of enzymatic hydrolysis ?-thionaphthylacetat display as the synergistic activator - in experiments with butyrylcholinesterase, and as the reversible inhibitor - in experiments with acetylcholineste­rase. Kinetic constants in reaction of acetylcholinesterase inhibition by cetyltrimethyl­ammonium defined by means of different substrates - ?-thionaphthylacetat and acetylthiocholin. They are close among themselves and amount (2.5 ± 0.3)?10-5 and (2.8 ± 0.3)?10-5 М, accordingly. Butyrylcholinesterase was more sensitive to influence of cetyltrimethylammonium. The kinetic constants defined for this enzyme by the effect of inhibition of acetylthiocholin hydrolysis or activation of ?-thionaphthylatcetat hydrolysis, are also close among themselves and amount (3.9 ± 0.4)?10-6 and (4.4 ± 0.4)?10-6 М, accordin­gly.

Key words: ?-thionaphtylacetat, acetylthio­choline, enzymatic hydrolysis, cetyltrimethylammonium, activation, inhibition, human erythrocyte acetylcholinesterase, human plasma butyrylcholinesterase.

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