Abstract
The flavin-containing monooxygenase has been purified from rabbit liver and lung microsomes. SDS-PAGE analysis shows that both enzyme forms migrate as a single band with an apparent Mr of 59000. The NH2-terminus of both forms is blocked. The liver oxidase contains a lower percentage of glutamine/glutamate and a greater amount of phenylalanine than does the lung flavoprotein. Polyclonal antibodies to a 14-amino-acid peptide obtained after CNBr cleavage of the liver oxidase cross-react with the microsomal and purified liver enzyme, but do not recognize the lung oxidase. HPLC profiles of tryptic digests of the liver and lung enzymes exhibit different patterns. Sequence alignment of selected peptides from the liver and lung oxidases reveals aberrant residues within homologous segments. These findings are interpreted to mean that both enzymes represent distinct gene products.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
