title: Study of properties of phosphorylase kinase using hydrophobic chromatography.
abstract: The structure of nonactivated and activated forms of phosphorylase kinase has been investigated. The enzyme activation was achieved by phosphorylation with cAMP-dependent protein kinase as well as by incubation of the enzyme in an alkaline medium (pH 8.8). For structural comparison of the enzymic forms, hydrophobic chromatography on phenyl-Sepharose and polyacrylamide gel electrophoresis were used. It has been shown that the enzyme activation results in a release of a low molecular weight component (Mr 16 000). The properties of this component resemble those of calmodulin. Evidence for the formation of an unstable nonactivated phosphorylase kinase - calmodulin complex may be important for the correct understanding of the mechanism of enzyme activation.
mesh_terms: D000818:Animals; D002847:Chromatography, Agarose; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010764:Phosphorylase Kinase / Q000032:analysis*; D011817:Rabbits
chemical_list: D010764:Phosphorylase Kinase