NAD+-dependent retinol dehydrogenase in liver microsomes

Maria Anna Leo, Cho Il Kim, Charles S. Lieber

Research output: Contribution to journalArticlepeer-review

70 Scopus citations

Abstract

A microsomal NAD+-dependent retinol dehydrogenase is being described with optimal activity at physiological pH. The enzyme was present in liver microsomes of rats and also in a strain of deermice which lacks the cytosolic retinol dehydrogenase. Unlike the latter enzyme, the microsomal retinol dehydrogenase was not inhibited by either ethanol or 4-methylpyrazole; its activity was insensitive to CO and not oxygen dependent, in contradistinction with that of the microsomal cytochrome P-450 and NADPH-dependent retinol oxidase. Chronic ethanol consumption resulted in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in view of the insensitivity of the enzyme to ethanol inhibition.

Original languageEnglish
Pages (from-to)241-249
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume259
Issue number2
DOIs
StatePublished - Dec 1987

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