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• W1500902011 abstract "An enzyme system capable of oxidizing both methanol and ethanol in the presence of DPN was purified almost ninety-fold from the liver of the rhesus monkey. Data for the km values for the two alcohols and DPN and for the Kivalues in the presence of some inhibitors are presented. The enzyme appears to be identical to liver alcohol dehydrogenase (ADH). Ethanol competitively inhibited the oxidation of methanol by this enzyme. The purified enzyme had appreciable activity when, in place of DPN, TPN was used as the hydrogen-acceptor. Contrary to the observations of earlier authors, crystalline ADH, purified from horse liver, had an appreciable activity with methanol as substrate. The data on the elimination of methanol in the blood of monkeys administered methanol by stomach tube agrees with the rates of its oxidation, as observed in vitro. It is concluded that the dehydrogenase mechanism, and not the catalase-peroxide system, is responsible for the physiological oxidation of methanol." @default.
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• W1500902011 date "1961-09-01" @default.
• W1500902011 modified "2023-09-26" @default.
• W1500902011 title "Biochemistry of methanol poisoning—III" @default.
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• W1500902011 doi "https://doi.org/10.1016/0006-2952(61)90003-x" @default.
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