Inactivation of alcohol and retinol dehydrogenases by acetaldehyde and formaldehyde.

The rapid and progressive inactivation of alcohol dehydrogenase from horse liver, rat liver and from human retina and of retinol dehydrogenase of rat liver by low concentrations of acetaldehyde or formaldehyde is illustrated. The inactivation of alcohol dehydrogenase can be largely prevented and partially reversed with glutathione. These findings are discussed as a model for better understanding of toxic effects of alcohol and in the context of the importance of protein turnover measurements for clarification of untoward alcohol effects.