| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9921039 | European Journal of Pharmacology | 2005 | 4 Pages |
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.
Related Topics
Life Sciences
Neuroscience
Cellular and Molecular Neuroscience
Authors
Munetaka Negoro, Ichiro Wakabayashi,