作者: Tasuku Asakawa , Kunio Itoh , Mayuko Adachi , Kouichi Hoshino , Nobuaki Watanabe
DOI: 10.1248/BPB.31.380
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摘要: We previously demonstrated the existence of a minor 130 kDa subunit in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)/Western blot analysis monkey liver cytosol and expressed aldehyde oxidase (AO) Escherichia coli. In contrast, was not observed rat AO. current study, properties were investigated from viewpoint species differences presence AO activity. Monkey with His-tag at N- C-terminus expressed, immunoanalyzed anti-AO anti-His-tag antisera. The results revealed that produced by cleavage N-terminal side 150 subunit. point shown to be located between 188Leu 189Pro Edman degradation method. two amino acids related are contained linkage 2Fe-2S FAD domains human monkey, but mouse. As fact, mouse, suggesting might one reason difference formation However, is associated activity, because loss cluster domain essential for exertion