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.
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