Characterization of expressed full-length and truncated FMO2 from rhesus monkey.

@article{Krueger2001CharacterizationOE,
  title={Characterization of expressed full-length and truncated FMO2 from rhesus monkey.},
  author={Sharon K. Krueger and Mei Fei Yueh and Sarah R Martin and Clifford B Pereira and David Edward Williams},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2001},
  volume={29 5},
  pages={693-700}
}
Flavin-containing monooxygenase (FMO) metabolizes a wide variety of nitrogen, sulfur, and phosphorous-containing xenobiotics. FMO2 is highly expressed in the lung of most mammals examined, but the protein has only recently been detected in humans, presumably due to a premature stop codon at AA472 in most individuals. In this study, full-length (mFMO2-535) and 3'-truncated (mFMO2-471) monkey FMO2 protein, produced by cDNA-mediated baculovirus expression, were characterized and compared with… CONTINUE READING