title: [Properties of phosphorylase kinase activated by subtilisin].
abstract: The activation of phosphorylase kinase during limited proteolysis by subtilisin was studied. It was shown that phosphorylase kinase undergoes rapid activation and its activity remains unchanged throughout a prolonged incubation. Electrophoresis in the presence of Na-SDS revealed a rapid decomposition of the alpha-subunit and a gradual disappearance of the beta-subunit; the protein molecule was shown to be composed of the degradation products of alpha- and beta-subunits with different molecular weights and unchanged proteolysis of the gamma-subunit. The phosphorylase kinase hydrolysate was separated using chromatography on a cellulose phosphate column. The active protein fraction contains a new form of phosphorylase kinase with a low molecular weight (approximately 80 000) which is insensitive to Ca2+. The subtilisin-activated phosphorylase kinase does not affect the activity of phosphodiesterase from cyclic nucleotides.
mesh_terms: D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004789:Enzyme Activation; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000378:metabolism*; D011817:Rabbits; D013381:Subtilisins / Q000378:metabolism*
chemical_list: D046911:Macromolecular Substances; D010764:Phosphorylase Kinase; D013381:Subtilisins; D002118:Calcium
vernacular_title: Svoistva kinazy fosforilazy, aktivnorovannoĭ subtilizinom.