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. Author manuscript; available in PMC: 2012 Jun 20.
Published in final edited form as: Chem Res Toxicol. 2011 Apr 18;24(6):797–808. doi: 10.1021/tx100447k

Table 1.

Bimolecular rate constants (ki) for inhibition of human AChE and BChE at pH 8.0 and 25°C.

AChE a BChE
Enzyme form E E′ E E′
ki (M−1min−1) 10% MeOH >3.7×106(b) (1.06±0.23)×105 (1.5±0.2)×108 (2.5±0.7)×107
ki (M−1min−1) 5% acetonitrile ND (0.33±0.17)×105 ND ND
ki (M−1min−1) 0.9% saline ND (0.73±0.6)×105 ND ND

E, enzyme fast forms; E′ enzyme slow forms

ND, not determined

Experiments were performed in triplicate (mean values ± SE)

a

experimental ki values for the E-form of AChE are not listed because the kinetics did not provide a second order rate constant in that instance.

b

estimated minimum ki value using kp= 0.37 min−1 and KI≪0.1 μM