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  • Title: [Properties of phosphorylase kinase activated by subtilisin].
    Author: Shur SA, Pegrova AN, Skolysheva AN, Vul'fson PL.
    Journal: Biokhimiia; 1981 Feb; 46(2):214-21. PubMed ID: 7018593.
    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.
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