Abstract
tracts of biotin-deficlent rat liver carboxylated propionate at a greatly reduced rate, highly purified preparations of propionyl carboxylase from pig heart were assayed for biotin;2 however, none was detected at that time. A reinvestigation of this problem was prompted by the finding that preparations of acetyl4 and A-methylcrotonyl5 carboxylase from liver and a bacterial source, respectively, contained biotin and were inactivated by avidin, the biotin-binding protein of egg white. The reactions catalyzed by these enzymes-carboxylation of acetyl CoA to malonyl CoA and of f-methylcrotonyl CoA to 3-methylglutaconyl CoA-conform to the pattern of reaction 1.6 It appeared, therefore, that propionyl carboxylase must contain
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.
