[Interaction between glycogen phosphorylase b and creatinine kinase from rabbit skeletal muscle].

Phosphorylase b association with creatine kinase has been studied by frontal elution affinity chromatography, using CNBr-Sepharose 4B immobilized creatine kinase as the affinity matrix. The quantitative parameters of this interaction were estimated from the volumes of phosphorylase b elution at various concentrations of the enzyme. The dissociation constants for phosphorylase b complexes with immobilized creatine kinase and of the phosphorylase b complex with free creatine kinase were found to be equal to 0.49 and 0.191 microM, respectively. In the presence of AMP the interaction between the proteins became weaker. With a rise in AMP concentration from 0.02 to 0.15 mM the value of the dissociation constants increased from 1.59 up to 9.66 microM. One molecule of AMP was shown to bind on the phosphorylase b-immobilized creatine kinase complex.