Enhancement of alcohol dehydrogenase activity in vitro by acetylsalicylic acid.
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.
Negoro
Munetaka
M
Department of Hygiene and Preventive Medicine, Yamagata University School of Medicine, Iida-Nishi 2-2-2, Yamagata 990-9585, Japan.
Wakabayashi
Ichiro
I
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000494:pharmacology*; D001241:Aspirin / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D000431:Ethanol / Q000378:metabolism; D006736:Horses; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D013997:Time Factors
D000894:Anti-Inflammatory Agents, Non-Steroidal; D000431:Ethanol; D000426:Alcohol Dehydrogenase; D001241:Aspirin