Interaction of calmodulin and glycogen phosphorylase.
We have demonstrated the interaction of 125I-labeled calmodulin with glycogen phosphorylase by four techniques: polyacrylamide gel overlay, sucrose density centrifugation, gel filtration chromatography, and affinity chromatography. Phosphorylase b has more affinity for calmodulin than does phosphorylase a. Under all conditions tested, the presence of calmodulin affects neither the enzymatic activity nor any kinetic characteristics of phosphorylase a or b. We present these results as evidence that while binding between calmodulin and phosphorylase clearly exists, it may not have a physiological role.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D010762:Phosphorylase a / Q000378:metabolism; D010763:Phosphorylase b / Q000378:metabolism; D006005:Phosphorylases / Q000378:metabolism*; D011485:Protein Binding
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010762:Phosphorylase a; D010763:Phosphorylase b; D006005:Phosphorylases; D015105:3',5'-Cyclic-AMP Phosphodiesterases