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J. Biochem, 1996, Vol. 119, No. 4 617-625
© 1996 Japanese Biochemical Society

research-article

Microsomal Aldehyde Oxygenase (MALDO): Purification and Characterization of a Cytochrome P450 Isozyme Responsible for Oxidation of 9-Anthraldehyde to 9-Anthracenecarboxylic Acid in Monkey Liver1

Tamihide Matsunaga*, Yasuyuki Iwawaki*, Kazuhito Watanabe*, Ikuo Yamamoto*,2, Takashi Kageyama{dagger} and Hidetoshi Yoshimura{ddagger}

*Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11
{dagger}Department of Biochemistry, Primate Research Institute, Kyoto University Inuyama 484
{ddagger}Department of Food and Nutrition, Nakamura Gakuen University Fukuoka 814-01

2To whom correspondence should be addressed. Tel: + 81-762-29-1165 (Ext. 345), Fax: +81-762-29-2781

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 P460JM-C, which mediate the oxidative biotransforma-tion 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-P460JM-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.

1This work was partially supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, and by the Special Research Fund of Hokuriku University.


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