@article{oai:tohoku-mpu.repo.nii.ac.jp:00000731,
 author = {伊藤, 邦郎 and Itoh, Kunio},
 issue = {64},
 journal = {東北医科薬科大学研究誌, Journal of Tohoku Medical and Pharmaceutical University},
 month = {Dec},
 note = {Aldehyde oxidase（AO）is a major member of the xanthine oxidase family belonging to the class of complex molybdo-flavoenzymes and plays an important role in the nucleophilic oxidation of N-heterocyclic aromatic compounds as well as various aldehydes. AO is homodimers with a subunit molecular weight of about 150 kDa and exhibit catalytic activity only as a dimer. An AO subunit contains a molybdopterin cofactor, an FAD and two different 2Fe-2S redox centers. The enzyme catalyzes oxidation of a wide range of endogenous and exogenous aldehydes and N-heterocyclic aromatic compounds.
The enzyme has been well known to show remarkable species differences. When the enzyme is focused on rabbit and monkey, the former showed extremely high activity towards cinchonidine and methotrxate but the latter exhibited only marginal activities. In contrast, monkey had several times greater activity than did rabbit towards zonisamide and（S）-RS-8359. In addition, marked differences in species, large differences in rat strains and individual differences of AO activities in some rat strains have been reported. However, little has been elucidated about any related molecular biological mechanisms. We examined the mechanism of individual variations, strain and species difference of AO using the technology of molecular biology.
Our recent studies regarding the inter- and intra-species difference of Ao activities are described in this review.},
 pages = {29--38},
 title = {アルデヒドオキシターゼの種差，個体差の解析},
 year = {2017},
 yomi = {イトウ, クニオ}
}