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  • Title: Phosphorylation and inactivation of brain glycogen synthase by a multifunctional calmodulin-dependent protein kinase.
    Author: Inoue N, Iwasa T, Fukunaga K, Matsukado Y, Miyamoto E.
    Journal: J Neurochem; 1987 Mar; 48(3):981-8. PubMed ID: 3100725.
    Abstract:
    Glycogen synthase was partially purified from canine brain to about 70% purity. The purified enzyme showed differences from the properties of the skeletal muscle enzyme with respect to molecular weights of the holoenzyme and subunit and phosphopeptide mapping. The multifunctional calmodulin-dependent protein kinase from the brain phosphorylated brain glycogen synthase with concomitant inactivation of the enzyme. Although about 1.3 mol of phosphate/mol subunit was maximally incorporated into glycogen synthase, 0.4 mol of phosphate/mol subunit was sufficient for the maximal inactivation of the enzyme. The results indicate that brain glycogen synthase is regulated in a calmodulin-dependent manner similarly to the skeletal muscle enzyme, but that the brain enzyme is different from the skeletal muscle enzyme.
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