Abstract
Branched-chain 2-oxo acid dehydrogenase kinase was characterized using anti-kinase polygonal antibodies. The antibodies were purified from rabbit antiserum by an epitope selection method. The antibodies bound only to a 44 kDa polypeptide in the dehydrogenase—kinase complex and inhibited the kinase activity, substantiating that the 44 kDa polypeptide is the catalytic subunit of the kinase. The purified liver dehydrogenase—kinase complex, but not either the purified heart complex or the partially purified liver complex, contained 2 additional polypeptides of lower molecular weight which also reacted with the anti-kinase antibodies, suggesting that the liver kinase is subject to proteolytic degradation during purification.
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.
