NAD+-dependent retinol dehydrogenase in liver microsomes

M. A. Leo; C. S. Lieber

doi:10.1016/0076-6879(90)89330-K

NAD⁺-dependent retinol dehydrogenase in liver microsomes

M. A. Leo, C. S. Lieber

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Abstract

This chapter discusses NAD⁺-dependent retinol dehydrogenase in liver microsomes. It also discusses the factors affecting the microsomal NAD+-dependent retinol dehydrogenase (MRD) activity. MRD has been described with optimal activity at physiological pH. The enzyme is present in liver microsomes of rats and in a strain of deermice that lacks the cytosolic retinol dehydrogenase (CRD). Unlike the latter enzyme, MRD is not inhibited by either ethanol or 4-methylpyrazole; its activity is insensitive to CO and is not oxygen dependent, in contradistinction with that of the microsomal cytochrome P-450 and NADPH-dependent retinol oxidase. Repeated freezing and thawing strikingly affect the enzyme activity.

Original language	English
Pages (from-to)	520-524
Number of pages	5
Journal	Methods in Enzymology
Volume	189
Issue number	C
DOIs	https://doi.org/10.1016/0076-6879(90)89330-K
State	Published - 1 Jan 1990

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title = "NAD+-dependent retinol dehydrogenase in liver microsomes",

abstract = "This chapter discusses NAD+-dependent retinol dehydrogenase in liver microsomes. It also discusses the factors affecting the microsomal NAD+-dependent retinol dehydrogenase (MRD) activity. MRD has been described with optimal activity at physiological pH. The enzyme is present in liver microsomes of rats and in a strain of deermice that lacks the cytosolic retinol dehydrogenase (CRD). Unlike the latter enzyme, MRD is not inhibited by either ethanol or 4-methylpyrazole; its activity is insensitive to CO and is not oxygen dependent, in contradistinction with that of the microsomal cytochrome P-450 and NADPH-dependent retinol oxidase. Repeated freezing and thawing strikingly affect the enzyme activity.",

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AB - This chapter discusses NAD+-dependent retinol dehydrogenase in liver microsomes. It also discusses the factors affecting the microsomal NAD+-dependent retinol dehydrogenase (MRD) activity. MRD has been described with optimal activity at physiological pH. The enzyme is present in liver microsomes of rats and in a strain of deermice that lacks the cytosolic retinol dehydrogenase (CRD). Unlike the latter enzyme, MRD is not inhibited by either ethanol or 4-methylpyrazole; its activity is insensitive to CO and is not oxygen dependent, in contradistinction with that of the microsomal cytochrome P-450 and NADPH-dependent retinol oxidase. Repeated freezing and thawing strikingly affect the enzyme activity.

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NAD+-dependent retinol dehydrogenase in liver microsomes

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NAD⁺-dependent retinol dehydrogenase in liver microsomes