Abstract
The effects of mixed function oxidase substrates, aminopyrine and ethylmorphine, on the NADPH and O2 dependent rate of ethanol oxidation have been examined. Aminopyrine like ethylmorphine exerts different effects on the rate of acetaldehyde formation depending upon the ethanol concentration used. At saturating ethanol concentration V max increases. Inhibition is observed at low concentrations of ethanol. Plots of acetaldehyde formation versus ethanol concentration reveal, in the presence of aminopyrine, curves which indicate the simultaneous action of two enzymes functional in ethanol oxidation. These data provide support for the existence of a microsomal ethanol oxidizing enzyme system (Orme-Johnson et al., 1965; Lieber et al., 1970), in addition to the well documented azide sensitive and H2O2 dependent pathway for ethanol oxidation (Thurman et al., 1972; Feytmans et al., 1973).
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