Kinetics of total enzymatic hydrolysis of acetylcholine and acetylthiocholine.
Kinetics and the mechanism of total in vitro hydrolyses (i.e. up to the exhaustion of substrate) of acetylcholine and acetylthiocholine by acetylcholinesterase and butyrylcholinesterase were studied in vitro in a batch reactor at 25 degrees C, pH 8 and ionic strength of 0.11 M. Every hydrolysis was monitored by 2-3 independent analytical methods. All studied types of enzymatic hydrolyses fulfilled the Michaelis-Menten reaction scheme with the irreversible second step. A table of obtained average values of rate constants and estimations of initial molar enzyme concentrations, and discussion of the results are presented.
Zdrazilová
Pavla
P
Faculty of Chemical Technology, Department of Physical Chemistry, University of Pardubice, Czech Republic.
Stepánková
Sárka
S
Vránová
Martina
M
Komers
Karel
K
Komersová
Alena
A
Cegan
Alexander
A
D000109:Acetylcholine / Q000378:metabolism*; D000110:Acetylcholinesterase / Q000097:blood / Q000378:metabolism*; D000122:Acetylthiocholine / Q000378:metabolism*; D000818:Animals; D002091:Butyrylcholinesterase / Q000378:metabolism*; D002417:Cattle; D004912:Erythrocytes / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D013053:Spectrophotometry; D013379:Substrate Specificity
D000122:Acetylthiocholine; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase; D000109:Acetylcholine