Abstract
In a previous paper' we reported that acetyl CoA carboxylase (E.C. 6.4.1.2) isolated in homogeneous form from chicken liver is an unusually large and asymmetric protein structure. The enzyme (in phosphate buffer, pH 7) has a molecular weight of about 8 million and a sedimentation coefficient of 53-58S. Its characteristic filamentous structure, revealed by electron microscopy, was easily dissociated into subunits with concomitant loss of enzymatic activity. Active filaments (70-100 A X up to 4000 A) were rapidly reconstituted by addition of isocitrate or other triand dicarboxylic acid anions. The present paper provides a more complete physicalchemical characterization of the protomeric and polymeric forms of acetyl CoA carboxylase, as well as an insight into the reversible dissociation-reassociation process and its relation to catalytic activity.
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.
