Abstract
2-Fluoroethanol, known to be toxic to rats, causes a considerable rise in tissue concentrations of citrate. Guinea-pig-kidney-particle preparations are unaffected by 2-fluoroethanol, which, however, is converted by incubation with liver slices or by coupled oxidation by catalase into a compound capable of inducing citrate in the particle preparations. Rat-liver slices oxidize 2-fluoroethanol to fluoroacetate, identified as the methyl ester by gas-liquid chromatography. 2-Fluoroethanol is not a substrate for crystalline horse-liver alcohol dehydrogenase, and competitively inhibits the oxidation of ethanol by this enzyme. A second liver alcohol dehydrogenase of different specificity readily oxidizes 2-fluoroethanol with nicotinamide-adenine dinucleotide, and to a lesser extent nicotinamide-adenine dinucleotide phosphate, as coenzymes. Fluoroacetaldehyde is oxidized 1.5 times as fast as is acetaldehyde by liver aldehyde dehydrogenase.