Abstract
The interaction of acetylsalicylic acid with alcohol dehydrogenase was investigated. Horse liver alcohol dehydrogenase bound to a p-hydroxyacetophenone affinity column was eluted by acetylsalicylic acid. In vitro enzymatic activity of alcohol dehydrogenase in the presence of ethanol as a substrate was significantly increased by incubation with acetylsalicylic acid. These results suggest that acetylsalicylic acid has an affinity with alcohol dehydrogenase and enhances its activity.
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Schedule a callMore From: European Journal of Pharmacology: Molecular Pharmacology
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