Phosphofructokinase is a calmodulin binding protein.
A trial to purify myosin light chain kinase from crude myosin led to the isolation of a Mr 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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D002846:Chromatography, Affinity; D003460:Crystallization; D005779:Immunodiffusion; D008970:Molecular Weight; D009219:Myosin-Light-Chain Kinase; D010732:Phosphofructokinase-1 / Q000302:isolation & purification / Q000378:metabolism*; D011494:Protein Kinases / Q000302:isolation & purification
D000596:Amino Acids; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins; D011494:Protein Kinases; D010732:Phosphofructokinase-1; D009219:Myosin-Light-Chain Kinase