Abstract
The effect of primaquine, chloroquine and other aminoquinoline derivatives on the enzymatic activity of crystalline horse liver alcohol dehydrogenase and partially purified human liver alcohol dehydrogenase has been studied. While chloroquine inhibits neither enzyme, primaquine inhibits both the horse and the human enzyme reversibly and noncompetitively with respect to NAD. The inhibition constant is 2 μM for the horse enzyme and 30 μM for the human enzyme. Spectrophotometric studies of the interaction of primaquine with the horse liver enzyme indicate that primaquine binds to a specific hydrophobic site on the protein. The stoichiometry of binding measured by spectrophotometric titrations is 2 moles primaquine/mole of enzyme and the dissociation constant of the complex is 3 μM. The effects of other 8-amino-6-methoxyquinoline compounds upon horse and human liver alcohol dehydrogenases suggest that the aliphatic side chain, as well as the terminal primary amino group of the side chain, contributes importantly to the tight binding of primaquine to these enzymes.
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