Ascorbic acid and alcohol oxidation.
Methanol and ethanol were rapidly metabolized to formaldehyde and acetaldehyde in the presence of ascorbate, 1,10-phenanthroline and either guinea pig hepatic 100,000 g supernatant or 12,000 g pellet fractions. The specific activity of methanol oxidation was 1720 nmoles formaldehyde formed/min/mg protein in the 100,000 g fraction and 790 in the 12,000 g pellet fraction. The specific activity of ethanol oxidation was 1590 nmoles acetaldehyde formed/min/mg protein in the 100,000 g fraction and 820 in the 12,000 g pellet fraction. The activity was enzymatic in that it was linear with time, proportional to protein concentration, and sensitive to temperature. Catalase appeared to be the enzymatic component responsible for the oxidation. In this ascorbate-dependent alcohol oxidation system, oxygen was consumed and H2O2 was formed. When purified catalase and ascorbate were used, complex I was detected and methanol was oxidized.
D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology*; D002374:Catalase / Q000032:analysis; D000431:Ethanol / Q000378:metabolism*; D006168:Guinea Pigs; D006861:Hydrogen Peroxide / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D008297:Male; D000432:Methanol / Q000378:metabolism*; D010084:Oxidation-Reduction; D010101:Oxygen Consumption
D000431:Ethanol; D006861:Hydrogen Peroxide; D002374:Catalase; D001205:Ascorbic Acid; D000432:Methanol