Cloning, Expression, and Characterization of Male Cynomolgus Monkey Liver Aldehyde Oxidase(Biochemistry)

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概要

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• In this study, we investigated the properties of monkey liver aldehyde oxidase directed toward the clarification of species differences. The aldehyde oxidase preparation purified from male cynomolgus monkey liver cytosol showed a major 150 kDa Coomassie brilliant blue (CBB)-stained band together with a minor 130 kDa band using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Both bands were identified as being aldehyde oxidase by a database search of the MS data obtained with nano-liquid chromatography, quardrupole time of flight, mass spectrometry (nano-LC Q/TOF MS). Based on the sequence coverage, the 130 kDa protein was presumed to be deficient in 20-30 kDa mass from the A'-terminus. Full male cynomolgus monkey aldehyde oxidase cDNA was cloned and sequenced with the four degenerate primers designed by considering the peptide sequences containing the amino acids specific for monkey aldehyde oxidase. The deduced amino acid sequences had 96% amino acid identity with those of human enzyme. The aldehyde oxidase expressed in Escherichia coli also exhibited two immunoreactive bands on SDS-PAGE/Western blot analysis. Further, the biphasic pattern was observed for Eadie-Hofstee plots of the (S)-enantiospecific 2-oxidation activity of RS-8359 with the expressed and cytosolic monkey liver aldehyde oxidase. The results suggested that two forms of aldehyde oxidase in monkey were the expression products by a single gene. In contrast, the similarly expressed rat aldehyde oxidase showed only one immunoreactive protein and monophasic pattern. The biphasic phenomenon could be caused by the existence of two aldehyde oxidase isoforms or two active sites in a single enzyme or some other reasons. Further studies on the problems of the biphasic pattern and species differences in aldehyde oxidase are needed.

• 公益社団法人日本薬学会の論文
• 2007-07-01

著者

• Tanaka Y

  Kyushu Univ. Fukuoka Jpn

• Watanabe Nobuaki

  Drug Metabolism And Pharmacokinetics Research Laboratories Daiichi-sankyo Co. Ltd.

• Watanabe Naomi

  Department Of Analytical Chemistry Faculty Of Pharmaceutical Sciences Hokuriku University

• Itoh K

  Department Of Pharmaceutical Sciences Tohoku University Hospital And Division Of Clinical Pharmacy G

• Itoh Kunio

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• Adachi Mayuko

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• Tanaka Y

  Toho Univ. School Of Pharmaceutical Sci. Chiba Jpn

• Tanaka Yorihisa

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• ASAKAWA Tasuku

  Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University

• HOSHINO Kouichi

  Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University

• MASUBUCHI Akiko

  Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University

• KOSAKA Toshiyuki

  Core Technology Research Laboratories, Sankyo Co., Ltd.

• Asakawa Tasuku

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• Masubuchi Akiko

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• Hoshino Kouichi

  Department Of Drug Metabolism And Pharmacokinetics Tohoku Pharmaceutical University

• Kosaka Toshiyuki

  Core Technology Research Laboratories Sankyo Co. Ltd.

• Tanaka Yorihisa

  Department Of Applied Chemistry National Defense Academy

• Kosaka Toshiyuki

  Core Technol. Res. Laboratories Sankyo Co. Ltd.

• Tanaka Yoshitaka

  Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University

• Itoh Kunio

  Department of Biopharmaceutics, Tohoku Pharmaceutical University

• Watanabe Nobuaki

  Drug Metabolism and Pharmacokinetics Research Laboratories, Daiichi-Sankyo Co., Ltd.

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