ISSN:
1573-9171
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Conclusions 1. Among the 17 carboxylic acid thioesters of derivatives morpholine, α-, β-, and γ-pipecoline studied, 10 were found to be substrates for acetylcholinesterase (ACE) and butyrylcholinesterase (BuCE), 6 were reversible inhibitors of these two enzymes, and one was hydrolyzed by the action of BuCE only. In all cases, the rates of hydrolysis of the substrates were lower than those for acetylthiocholine. 2. Comparison of the kinetic parameters of the hydrolysis of several oxygen substrates and analogs specific for ACE showed that when the ester O atom is replaced by S, the specificity of the substrates with respect to ACE decreases because of decrease in the hydrolysis rate by the action of ACE and increase or retention at the same level of the rate of hydrolysis by the action of BuCE.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00954701
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