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Porcine liver phosphorylase kinase was activated about 1.5-fold by calmodulin in a calcium-dependent manner. Half-maximal stimulation was observed at about 80 nM calmodulin and the activation was almost pH-independent. The specific binding of procine liver phosphorylase kinase to calmodulin-Sepharose affinity column exhibited an absolute dependence upon the presence of calcium. The physiological role...