A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a ‘High‐Km,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism

Elizabeth M. Algar, John L. VandeBerg, Roger S. Holmes

    Research output: Contribution to journalArticle

    9 Scopus citations

    Abstract

    The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using Kcat/Km, values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed ‘high‐Km’ properties with respect to ethanol, and is expected to significantly contribute to ‘first‐pass’ metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver ‘low‐Km’ ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.

    Original languageEnglish (US)
    Pages (from-to)922-927
    Number of pages6
    JournalAlcoholism: Clinical and Experimental Research
    Volume16
    Issue number5
    DOIs
    StatePublished - Oct 1992

    Keywords

    • Alcohol Dehydrogenase
    • Baboon
    • Ethanol
    • Stomach

    ASJC Scopus subject areas

    • Medicine (miscellaneous)
    • Toxicology
    • Psychiatry and Mental health

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