The inhibitory effects of endogenous NADPH-pyrophosphatase on the reduction of cytochrome c and the oxidation of drugs by liver microsomes

NADPH-pyrophosphatase in rat liver converts NADPH to products which inhibit NADPH cytochrome c reductase. This reaction obscures studies on the K m (NADPH) for drug oxidation by liver microsomes from this species. Studies with mouse liver microsomes, which contain relatively little NADPH-pyrophospha...

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Published inArchives of biochemistry and biophysics Vol. 140; no. 1; pp. 113 - 121
Main Authors Sasame, Henry A., Gillette, James R.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.09.1970
Subjects
Adenine Nucleotides
Aminopyrine
Animals
Benzopyrenes
Cytochromes - metabolism
Diphosphates - metabolism
Guinea Pigs
Kinetics
Male
Mice
Microsomes, Liver - metabolism
NADP - metabolism
Oxidoreductases - metabolism
Phosphoric Monoester Hydrolases - metabolism
Rabbits
Rats
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Summary:NADPH-pyrophosphatase in rat liver converts NADPH to products which inhibit NADPH cytochrome c reductase. This reaction obscures studies on the K m (NADPH) for drug oxidation by liver microsomes from this species. Studies with mouse liver microsomes, which contain relatively little NADPH-pyrophosphatase, revealed that the K m (NADPH) for drug oxidation is less than 1 μ m; which is at least an order of magnitude lower than that reported for aminopyrine metabolism by rat liver microsomes.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(70)90015-9