Oxidation of Ethylene Glycol to Glycolaldehyde by Mammalian Tissues

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Abstract
The mammalianfenzymes oxidizing ethylene glycol to glycolaldehyde were investigated with homogenates of horse liver and of rat tissues. The oxidation was followed by measuring either pyridine nucleotide reduction by fluorometry or glycolaldehyde with diphenylamine. The reaction required either NAD+ or a biological source of H^jOj; NADP+ was ineffective. In the presence of NAD+, crude horse liver demonstrated the same relative rates for ethylene glycol oxidation, ethanol oxidation, and acetaldehyde reduction as did crystalline horse liver alcohol dehydrogenase. The oxidation of many flavoprotein oxidoreductase substrates (including glycolic acid, a metabolite of ethylene glycol) could be coupled to that of ethylene glycol, presumably by providing a source of H5O2 for the oxidation of ethylene glycol via tissue catalase. Partially purified L-gulonate: NADP oxldoreductase and glycerol: NADP oxldoreductase (D-glyceraldehyde forming) oxidized ethylene glycol poorly. The results suggest that the Important enzymes in the first step of ethylene glycol oxidation are the same as those for ethanol oxidation, namely alcohol dehydrogenase and catalase.

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