Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification.

Abstract

Aldehyde oxidase (EC 1.2.3.1) in monkey (Macaca fascicularis) liver was characterized. Liver cytosol exhibited extremely high benzaldehyde and phthalazine oxidase activities based on aldehyde oxidase, compared with those of rabbits, rats, mice and guinea pigs. Monkey liver aldehyde oxidase showed broad substrate specificity distinct from that of the enzyme from other mammals. Purified aldehyde oxidase from monkey liver cytosol showed two major bands and two minor bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These bands were also observed in Western blotting analysis using anti-rat aldehyde oxidase. The molecular mass of the enzyme was estimated to be 130-151 kDa by SDS-PAGE, and to be about 285 kDa by HPLC gel filtration. The results suggest that isoforms of aldehyde oxidase exist in monkey livers.

Cite this paper

@article{Sugihara2000CynomolgusML, title={Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification.}, author={Kenichi Sugihara and Yoshinori Katsuma and Shigeyuki Kitamura and Shoichiro Ohta and Morioki Fujitani and Hideaki Shintani}, journal={Comparative biochemistry and physiology. Toxicology & pharmacology : CBP}, year={2000}, volume={126 1}, pages={53-60} }