Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver.

Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Research Abstract Details 

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Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Abstract Text:

T Matsunaga,Y Iwawaki,K Watanabe,I Yamamoto,T Kageyama,H Yoshimura,

Oxidative activity of 9-anthraldehyde (9-AA) to 9-anthracenecarboxylic acid in monkey liver was mainly located in microsomes. The reaction required NADPH as an essential cofactor and was significantly inhibited by SKF 525-A, metyrapone, disulfiram, and CO, potent inhibitors of microsomal aldehyde oxygenase (MALDO). Two cytochrome P450 isozymes, named P450JM-A and P450JM-C, which mediate the oxidative biotransformation of 9-AA were purified from hepatic microsomes of untreated male and female Japanese monkeys, respectively. These isozymes each showed a single band of molecular mass 51,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The NH2-terminal amino acid sequences of P450JM-A and P450JM-C are highly homologous with those of several P450s belonging to the CYP2A and CYP2B subfamilies, respectively. The anti-P450JM-C antibody significantly suppressed 9-AA MALDO activity in monkey liver, but anti-P450JM-A antibody did not. The antibody against CYP2C11, which is a major isozyme responsible for 9-AA MALDO in male rat liver, also inhibited the activity. These results indicate that P450JM-C and isozyme(s) immunologically related to CYP2C11 predominantly possess MALDO activity toward 9-AA.

Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Publishing Authors By Initials

T Matsunaga,Y Iwawaki,K Watanabe,I Yamamoto,T Kageyama,H Yoshimura,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

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Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 119

Page Numbers: 617-25

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1996

Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Keywords Mesh Terms:

KEYWORDS: Sequence Homology, Amino Acid

MESH TERMS: metabolism

Chemical & Substance for Abstract: Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver. Information

Substance Name: coumarin 7-hydroxylase

Registry Number: EC 1.14.14.1

Grant and Affiliation Information for Microsomal aldehyde oxygenase (MALDO): purification and characterization of a cytochrome P450 isozyme responsible for oxidation of 9-anthraldehyde to 9-anthracenecarboxylic acid in monkey liver.

AFFILIATION: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa.

Country: JAPAN

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MEDLINETA: J Biochem

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