Abstract
Monoamine oxidase (MAO) of rat liver mitochondria was found to be inhibited by disulfiram. The inhibition is pH and time dependent: 50% inhibition was observed by 16.5 μM of disulfiram at pH 9.1 after 30 min of preincubation. At pH 7.4 only slight inhibition was produced despite the high concentration of disulfiram (330 μM) and the preincubation period. The inhibition is irreversible and appears to be of mixed type: noncompetitive at low concentration range of the substrate and uncompetitive at high concentration range. Glutathione at twice the concentration of disulfiram abolished the inhibitory effect of the drug. Ethanol, while by itself has only slight effect on MAO activity, enhanced the inhibitory effect of disulfiram at pH 7.4. At pH 9.1, ethanol alone has no effect on MAO; however, it was found to weaken the inhibitory effect of disulfiram.
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