caa a22 4500 397557302 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021287 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021287 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 [Elektronische Daten] [Tamihide Matsunaga, Yasuyuki Iwawaki, Kazuhito Watanabe, Ikuo Yamamoto, Takashi Kageyama, Hidetoshi 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 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. © by the Journal of Biochemistry Regular Papers nationallicence 9-anthraldehyde nationallicence cytochrome P450 nationallicence microsomal aldehyde oxygenase nationallicence monkey nationallicence purification nationallicence Matsunaga Tamihide Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut Iwawaki Yasuyuki Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut Watanabe Kazuhito Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut Yamamoto Ikuo Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut Kageyama Takashi Department of Biochemistry, Primate Research Institute, Kyoto University Inuyama 484 aut Yoshimura Hidetoshi Department of Food and Nutrition, Nakamura Gakuen University Fukuoka 814-01 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 617-625 0021-924X 119:4<617 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021287 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021287 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Matsunaga Tamihide Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut NATIONALLICENCE 700 1- Iwawaki Yasuyuki Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut NATIONALLICENCE 700 1- Watanabe Kazuhito Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut NATIONALLICENCE 700 1- Yamamoto Ikuo Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University Kanazawa 920-11 aut NATIONALLICENCE 700 1- Kageyama Takashi Department of Biochemistry, Primate Research Institute, Kyoto University Inuyama 484 aut NATIONALLICENCE 700 1- Yoshimura Hidetoshi Department of Food and Nutrition, Nakamura Gakuen University Fukuoka 814-01 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 617-625 0021-924X 119:4<617 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford