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Dissociation of Microsomal Ethanol Oxidation from Cytochrome P-450 Catalyzed Drug Metabolism

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 58))

Abstract

Considerable evidence is currently available which strongly suggests that, in addition to the alcohol dehydrogenase (ADH)-catalyzed reaction, a pyrazole-insensitive pathway participates in the metabolism of ethanol in vivo (Israel et al., 1970; Lieber and DeCarli, 1972), in the isolated perfused rat liver (Papenberg et al., 1970; Thurman and McKenna, 1974), in rat and mouse liver slices (Thieden, 1971; Lieber and DeCarli, 1970; Vatsis and Schulman, 1973a; Vatsis et al., 1973), and in isolated rat liver parenchymal cells (Grunnet et al., 1973). The non-ADH pathway has two distinguishing properties, namely, it becomes increasingly important at ethanol concentrations (20–80 mM) well above the Km of AHD (Thieden, 1971; Vatsis et al., 1973; Lieber and DeCarli, 1973), and appears to be inducible by chronic ethanol feeding (Lieber and DeCarli, 1970, 1972) as well as by treatment of animals with phenobarbital (Carter and Isselbacher, 1971; Khanna et al., 1972; Vatsis and Schulman, 1974).

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© 1975 Plenum Press, New York

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Vatsis, K.P., Schulman, M.P. (1975). Dissociation of Microsomal Ethanol Oxidation from Cytochrome P-450 Catalyzed Drug Metabolism. In: Cooper, D.Y., Rosenthal, O., Snyder, R., Witmer, C. (eds) Cytochromes P-450 and b5 . Advances in Experimental Medicine and Biology, vol 58. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9026-2_26

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  • DOI: https://doi.org/10.1007/978-1-4615-9026-2_26

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9028-6

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