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PMID:6223841

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Citation

Mayr, GW and Heilmeyer, LM Jr (1983) Phosphofructokinase is a calmodulin binding protein. FEBS Lett. 159:51-7

Abstract

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.

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PubMed

Keywords

Amino Acids/analysis; Animals; Calmodulin-Binding Proteins; Carrier Proteins/metabolism; Cattle; Chromatography, Affinity; Crystallization; Immunodiffusion; Molecular Weight; Myosin-Light-Chain Kinase; Phosphofructokinase-1/isolation & purification; Phosphofructokinase-1/metabolism; Protein Kinases/isolation & purification

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


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References

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