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• W2149945265 abstract "Two types of alcohol dehydrogenase isoenzymes (differing in their affinity for ethanol, sensitivity to 4-methylpyrazole, and electrophoretic migration) have been identified in the human stomach. At the high ethanol concentrations prevailing in the gastric lumen during alcohol consumption, the sum of their activities could account for significant oxidation of ethanol. In vitro, these activities were inhibited by cimetidine and ranitidine, but not by famotidine. In vivo, therapeutic doses of cimetidine (but not of famotidine) increased blood ethanol levels when ethanol was given orally, but not when it was given intravenously, indicating a significant contribution of the gastric ADH to the bioavailability and thereby the potential toxicity of ethanol." @default.
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• W2149945265 date "1990-12-01" @default.
• W2149945265 modified "2023-10-17" @default.
• W2149945265 title "Human Gastric Alcohol Dehydrogenase: Its Inhibition by H2-Receptor Antagonists, and Its Effect on the Bioavailability of Ethanol" @default.
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• W2149945265 doi "https://doi.org/10.1111/j.1530-0277.1990.tb01843.x" @default.
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