State of microsomal oxidation enzymes as a function of acetyltransferase activity

Quantity and activity of components in the monoxygenase system of the liver microsomes have been studied for their dependence on the phenotype of acetylation. Results of investigations are presented. The majority of these enzymes exist as numerous molecular forms: isozymes. It is shown that activity...

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Published inUkrainskij biohimičeskij žurnal Vol. 65; no. 6; p. 108
Main Authors Rudaia, N V, Syvachenko, O E, Alferov, A N, Bychkar', E M, Korzhov, V I
Format Journal Article
LanguageRussian
Published Ukraine 01.11.1993
Subjects
Acetyltransferases - genetics
Acetyltransferases - metabolism
Aminopyrine N-Demethylase - metabolism
Aniline Hydroxylase - metabolism
Animals
Cytochrome P-450 Enzyme System - metabolism
Female
Genetic Variation
Guinea Pigs
Isoenzymes - genetics
Isoenzymes - metabolism
Male
Microsomes, Liver - enzymology
Oxidation-Reduction
Phenotype
Steroid Hydroxylases - metabolism
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Summary:Quantity and activity of components in the monoxygenase system of the liver microsomes have been studied for their dependence on the phenotype of acetylation. Results of investigations are presented. The majority of these enzymes exist as numerous molecular forms: isozymes. It is shown that activity of aminopyrine-N-demethylase and NADPH-cytochrome P-450 reductase depends on the phenotype of acetyltransferase.
ISSN:0201-8470