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Hepatic microsomal ethanol oxidizing system (MEOS): Differentiation from alcohol dehydrogenase and NADPH oxidase

1970; Elsevier BV; Volume: 40; Issue: 4 Linguagem: Inglês

10.1016/0006-291x(70)90982-4

1090-2104

Charles S. Lieber, Emanuel Rubin, Leonore M. DeCarli,

Eicosanoids and Hypertension Pharmacology

Washed hepatic microsomes contain an active ethanol oxidizing system (MEOS) but no detectable ADH activity, even when 3-AP-NAD is used as a cofactor. ADH inhibitors (pyrazole and DMSO) failed to affect MEOS activity at concentrations which markedly reduced ADH activity. Therefore ADH is not a component of MEOS. Cholate, which inhibits the activities of both microsomal NADPH oxidase and MEOS, also strikingly diminishes that of other microsomal enzymes such as aniline hydroxylase and aminopyrine demethylase. Furthermore cholate inactivates both total and enzymatically reducible microsomal cytochrome P450. Thus, because of the non-specific nature of the inhibition by cholate, one cannot conclude from its effects that NADPH oxidase is a component of MEOS.