Characterization of the purified microsomal FAD-containing monooxygenase from mouse and pig liver.

@article{Sabourin1984CharacterizationOT,
  title={Characterization of the purified microsomal FAD-containing monooxygenase from mouse and pig liver.},
  author={P J Sabourin and Ernest Hodgson},
  journal={Chemico-biological interactions},
  year={1984},
  volume={51 2},
  pages={125-39}
}
The FAD-containing monooxygenase (FMO) has been purified from both mouse and pig liver microsomes by similar purification procedures. Characterization of the enzyme from these two sources has revealed significant differences in catalytic and immunological properties. The pH optimum of mouse FMO is slightly higher than that of pig FMO (9.2 vs. 8.7) and, while pig FMO is activated 2-fold by n-octylamine, mouse FMO is activated less than 20%. Compounds, including primary, secondary and tertiary… CONTINUE READING