Naslov
Inhibition of acetylcholinesterase by N-methylpyridinium derivatives

Autori
Škrinjarić-Špoljar, Mira ; Buntić, Anđelka ; Deljac, Vjera

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Godišnji sastanak hrvatskih biokemičara, Bizovačke Toplice, Sažeci znanstvenih priopćenja, ISBN953-6256-28-2 / Glavaš-Obrovac, Ljubica - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 1998

Skup
Annual Meeting of Croatian Biochemists with International Participation

Mjesto i datum
Bizovac, Hrvatska, 17.09.1998. - 20.09.1998

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
pyridinium compounds; 2-PAM; oximes; acetylcholinestrase inhibition

Sažetak
1-N-methylpyridinium iodide (I) and its three derivatives: 2-(hydroxyiminomethyl)-1-methylpyridinium iodide (2-PAM), 3-(hydroxy)-2-(hydroxyiminomethyl)-1-methylpiridinium iodide (II) and the dimethylcarbamate of compound II (III) were assayed for their inhibitory effect in vitro on the human blood acetylcholinesterase (EC 3.1.1.7, AChE). Compounds II and III were newly synthetized oximes. The enzyme activity was measured spectrophotometrically with substrate acetylthiocholine (ATCh) in the presence of the DTNB reagent, in 0.1 M phosphate buffer of pH 7.4. Compounds I, 2-PAM and II were reversible inhibitors of AChE. The dissociation constants of the enzyme/inhibitor complex for binding in the AChE catalytic site were evaluated from the relationships of the apparent dissociation constants vs low ATCh concentrations (up to 1.0 mM) and their values were between 0.3 and 1.9 mM. Compound I was found to bind also at the allosteric AChE binding site and the dissociation constant evaluated at high ATCh concentrations (1.0 to 10 mM) was 0.6 mM. Compound III was also a week AChE acylating inhibitor.

Izvorni jezik
Engleski

Znanstvena područja
Kliničke medicinske znanosti

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