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EFFECT OF ETHANOL ON THE OXIDATIVE METABOLISM OF TRYPTAMINE BY RAT LIVER HOMOGENATE
Author(s) -
ASAAD M.M.,
BARRY H.,
CLARKE D.E.,
DIXIT B.N.
Publication year - 1974
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1974.tb08573.x
Subject(s) - acetaldehyde , tryptamine , oxidative deamination , ethanol , chemistry , alcohol dehydrogenase , biochemistry , ethanol metabolism , metabolite , oxidative phosphorylation , nad+ kinase , enzyme
1 The effect of a wide range of ethanol concentrations (v/v) on indoleacetic acid (IAA) formation from the oxidative deamination of tryptamine was studied in vitro , in rat whole liver homogenate. 2 IAA production was inhibited progressively by ethanol in concentrations between 0.01% to 0.2%, but the inhibition declined when the ethanol concentration was increased further to 6%. 3 Ethanol‐induced inhibition of IAA formation was only partially reversed by excess aldehyde dehydrogenase, whereas reductions in IAA formation were completely prevented by pyrazole or ethanol (6% and 10%) itself. 4 Excess nicotinamide adenine dinucleotide failed to alter the inhibitory effect of ethanol and no evidence was obtained for inhibition of monoamine oxidase by ethanol or its metabolite, acetaldehyde. 5 We conclude that ethanol indirectly inhibits IAA production as a result of oxidation of ethanol by alcohol dehydrogenase, during which the oxidative metabolism of tryptamine is shifted towards the reductive pathway, thus favouring the formation of tryptophol in place of IAA.