Naslov
Peripheral binding of ethopropazine to horse serum butyrylcholinesterase

Autori
Reiner, Elsa ; Šinko, Goran ; Štuglin, Anita ; Simeon-Rudolf, Vera

Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni

Izvornik
Cholinergic mechanisms : Function and Dysfunction : Proceedings of the XIth ISCM / Fisher, Abraham ; Silman, Israel ; Soreq, Hermona ; Anglister, Lili ; Michaelson, Daniel M. - London : Delhi : Francis & Taylor, 2004, 673-674

ISBN
1841840750

Skup
XIth International Symposium on Cholinergic Mechanisms Function and Dysfunction and 2nd Misrahi Symposium on Neurobiology

Mjesto i datum
St. Moritz, Švicarska, 05.05.2002. - 09.05.2002

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
butyrylcholinesterase; ethopropazine; mechanism; inhibition

Sažetak
The inhibition of purified horse serum butyrylcholinesterase (BChE) with ethopropazine (0.25-20 uM) was studied in order to evaluate the binding site(s) on the enzyme. Activities were measured spectrophotometrically with acetylthiocholine (ATCh ; 0.05-80 mM) as substrate at 37º C in 0.1 M phosphate buffer pH=7.4. The pS-curve for the ATCh hydrolysis fitted well the Webb equation: Ks and Kss = 0.25 and 2.0 mM respectively, beta=3.2. This equation assumes two binding sites for the substrate on the enzyme, catalytic and peripheral, and the beta-value above unity indicates apparent substrate activation. Inhibition of BChE with ethopropazine was non-competitive at substrate concentrations up to 1.0 mM. The enzyme-inhibitor dissociation constant was 0.81 uM. Competition between ATCh and ethopropazine occured at substrate concentrations above the Kss value for ATCh. Such inhibition pattern indicates binding of ethopropazine to the peripheral, non-productive, site on the enzyme.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA