title: Kinetics of total enzymatic hydrolysis of acetylcholine and acetylthiocholine.
abstract: 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.
authors.affiliation: Faculty of Chemical Technology, Department of Physical Chemistry, University of Pardubice, Czech Republic.
authors.forename: Pavla
authors.initials: P
authors.lastname: Zdrazilová
authors.forename: Sárka
authors.initials: S
authors.lastname: Stepánková
authors.forename: Martina
authors.initials: M
authors.lastname: Vránová
authors.forename: Karel
authors.initials: K
authors.lastname: Komers
authors.forename: Alena
authors.initials: A
authors.lastname: Komersová
authors.forename: Alexander
authors.initials: A
authors.lastname: Cegan
mesh_terms: 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
chemical_list: D000122:Acetylthiocholine; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase; D000109:Acetylcholine