In vitro inhibition of cholinesterases by carbamates--a kinetic study.
Kinetics and mechanism of in vitro hydrolyses of acetylcholine and acetylthiocholine by carbamates were studied in a batch reactor at 25 degrees C, pH 8, and ionic strength of 0.11 M. Every hydrolysis was monitored by 3-4 independent methods. All studied hydrolyses can be described by the model of competitive inhibition with an irreversible step (k3). A table of obtained average values of rate constants and discussion of the resultes are given.
Komersová
Alena
A
Department of Physical Chemistry, Faculty of Chemical Technology, University of Pardubice, Nám. Legií 565, 532 10 Pardubice, Czech Republic. alena.komersova@upce.cz
Masopustová
Markéta
M
Komers
Karel
K
Stĕpánková
Sárka
S
Cegan
Alexandr
A
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002091:Butyrylcholinesterase / Q000378:metabolism*; D002219:Carbamates / Q000494:pharmacology*; D002800:Cholinesterase Inhibitors / Q000494:pharmacology*; D004593:Electrophorus; D007700:Kinetics
D002219:Carbamates; D002800:Cholinesterase Inhibitors; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase