Abstract
The inhibitory effects of 2-bromoethylamine (2-BEA), a derivative of ethylamine, on guinea pig lung semicarbazide-sensitive amine oxidase (SAO) have been studied. Preincubation with 2-BEA time-dependently inhibited SSAO activity. The mode of the initial phase of inhibition was competitive, with a Ki value of 52 microM. After preincubation at 37 degrees C for 2 h, the inhibition was noncompetitive and irreversible, as there was no recovery of SSAO activity by dilution of the inhibited samples. Kinetic analyses confirmed previous results with rat lung SSAO that 2-BEA is a suicide SSAO inactivator with a dissociation constant of 42 microM. This latter value is similar to that of the Ki value (52 microM) for the reversible phase of inhibition by 2-BEA. Addition of the nucleophilic compound 2-mercaptoethanol could not reduce the SSAO inhibition, indicating that inactivation could not be prevented by trapping the enzymatic reaction product from 2-BEA. This finding clearly indicates that the reaction product should not diffuse away from its site of genesis and agrees with one of the characteristics of suicide inhibitors. This conclusively excludes the possibility of an affinity-labeling mechanism.
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