Phosphofructokinase is a calmodulin binding protein

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Abstract
A trial to purify myosin light chain kinase from crude myosin led to the isolation of a M r 85 000 calmodulin binding protein different from this enzyme. Because it showed inherent phosphofructokinase activity we investigated its relation to this enzyme. We demonstrated identity to phosphofructokinase by a close to identical amino acid composition, by antigenic identity and a set of completely identical peptide maps. The calmodulin binding property was also shown for a fraction of the enzyme prepared by standard methods. First experiments show that Ca2+‐calmodulin is a potent regulator of phosphofructokinase polymerization.