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Titolo:
Interactions of rat brain acetylcholinesterase with the detergent Triton X-100 and the organophosphate paraoxon
Autore:
Rosenfeld, C; Kousba, A; Sultatos, LG;
Indirizzi:
Univ Med & Dent New Jersey, New Jersey Med Sch, Dept Physiol & Pharmacol, Newark, NJ 07103 USA Univ Med & Dent New Jersey Newark NJ USA 07103 acol, Newark, NJ 07103 USA
Titolo Testata:
TOXICOLOGICAL SCIENCES
fascicolo: 2, volume: 63, anno: 2001,
pagine: 208 - 213
SICI:
1096-6080(200110)63:2<208:IORBAW>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHOLINESTERASE; FORMS; BUTYRYLCHOLINESTERASE; SENSITIVITY; ENZYME; TISSUE;
Keywords:
paraoxon; acetylcholinesterase; organophosphate; pesticide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Sultatos, LG Univ Med & Dent New Jersey, New Jersey Med Sch, Dept Physiol & Pharmacol, 185 S Orange Ave, Newark, NJ 07103 USA Univ Med & Dent New Jersey 185 S Orange Ave Newark NJ USA 07103
Citazione:
C. Rosenfeld et al., "Interactions of rat brain acetylcholinesterase with the detergent Triton X-100 and the organophosphate paraoxon", TOXICOL SCI, 63(2), 2001, pp. 208-213

Abstract

Inhibition of the critical enzyme acetylcholinesterase (E.C. 3.1.1.7) withsubsequent cholinergic crisis is the mechanism of acute toxicity of the organophosphorus insecticides (B. E. Mileson et al.,1998,Toxicol. Sci.41, 8-20). Consequently, measurement of acetylcholinesterase activity is importantfor evaluating the mammalian toxicity of this commonly used class of insecticides. While mammalian acetylcholinesterase activity has often been determined in tissue homogenates in the presence of the nondenaturing detergent Triton X-100 at a concentration of 1%, the potential actions of this detergent on the activity of this critical enzyme are not understood. In the current study, homogenization of rat brain in buffer containing 1% Triton X-100slightly elevated the(app)V(max)for hydrolysis of acetylthiocholine, without affecting the(app)K(m)or the(app)K(ss). However, the presence of both 1%Triton X-100 and paraoxon (at concentrations of 5 nM-100 nM) resulted in complex kinetic interactions with acetylcholinesterase, as evidenced by a curvilinear secondary plot for determination of the(app)k(i). These results suggest that measurement of acetylcholinesterase activity in the presence ofup to 1% Triton X-100, but in the absence of oxon, should pose no problemswith regard to data interpretation, provided it is recognized that the detergent slightly elevates activity. However, measurement of acetylcholinesterase activity after enzyme was exposed simultaneously to Triton X-100 and oxon could be problematic. Caution is warranted when interpreting data whereacetylcholinesterase activity was determined under such conditions since in the presence of 1% Triton X-100, the capacity of oxon to inhibit acetylcholinesterase might change as a function of oxon levels.

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Documento generato il 03/04/20 alle ore 10:07:50