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The importance of steric and stereochemical features in serum cholinesterase substrates

Authors
Journal
Biochemical Pharmacology
0006-2952
Publisher
Elsevier
Publication Date
Volume
17
Issue
8
Identifiers
DOI: 10.1016/0006-2952(68)90221-9
Disciplines
  • Biology

Abstract

Abstract Rates of hydrolysis of the optical isomers of the butyryl-α and β-methylcholines of known configuration have been determined by using purified horse serum cholinesterase, horse and human serum † † Typical human serum. . Inhibition of serum esterase activity toward butyrylcholine as substrate by using benzoylcholine, p-aminobenzoylcholine and the opticali somers of p-aminobenzoyl-α and β-methylcholine is described. The similarity between horse and human serum esterase is discussed and a probable common identity is suggested for the active sites in the mixture of enzymes of serum cholinesterase of a given species.

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