ASCORBIC AClD AND ALCOHOL QXfDAl-‘lON*

A~~~e~-Met~an~ ~ and ethanol were rapidly metabolized to formaldehyde and a~etaldebyd ~ in the ~reseuce of ascorbatG ~,l~-pben~tb~~~~ne and either guinea pig hepatic l~,~ ~ supernatal % or ~~,~~ ~ p&et fractions. The specific activity of methanoi oxidation was 1720 amoles fo~a~deb~d~ ~orrne~m~~m ~ protein in the ~~,~ ~ fraction and 790 ii3 the WBO g p&et fraction. The specific activity of erhanaf oxidation was l.590 nmoies acetaldehjde forrn~~~~~‘rng protein in the ~~*~~ fmclion and 8 % in the ~~,~~ ~ p&et fraction. Ke activity was enzymatic in that it was linear with time, proportional to protein concentration, and sensitive to temperature. Catalasc appeared to be the enzymatic component responsible for the oxidation. In this ascorbate-dependent alcohol oxidstiott system, oxygen was consumed and W,O, was formed. When purified cataiase and ascorbate were ui;ed, complex I was detected and methanol was oxidized. There are three p~~~~pl ~ etrzymatic ~~th~a~s capable of oxidizing methanol or ethanol to thetr respective aldehydes [I), These include cyfosohc alcohol ~~h~drogenase (AI%, EC 1.1.Il+l) whicfi utilizes NAD*, cytosolic and peroxisomal cat&s