Abstract
Substituted phenyl-N-butylcarbamates ( 1) as active site-directed irreversible inhibitors of pancreatic cholesterol esterase are investigated for values of the dissociation constant (K I), the carbamylation constant (k 2), and the bimolecular rate constant (k i). Linear free energy relationships between-logK I, logk 2, or logk i and substituent constant (σ) are observed.
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