RT Journal Article
SR Electronic
T1 Structural Specificity of Substrates of Acetylcholinesterase
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 103
OP 107
VO 3
IS 2
A1 J. THOMAS
A1 B. D. ROUFOGALIS
YR 1967
UL http://molpharm.aspetjournals.org/content/3/2/103.abstract
AB 1(2-Acetoxyethyl)quinuclidinium iodide has been examined as a substrate of both purified acetylcholinesterase and human serum cholinesterase. Neither enzyme is capable of hydrolyzing it. The inhibition of acetylcholinesterase by the quinuclidine ester has been investigated and the Ki is reported. The stability of the ester toward acetylcholinesterase is discussed in terms of the molecular perturbation theory of drug action. ACKNOWLEDGMENT This investigation was supported in part by grants from the National Health and Medical Research Council of Australia. The authors wish to thank Mr. B. K. Williams for assistance with the chemical work.