Phosphorylation and Inactivation of Brain Glycogen Synthase by a Multifunctional Calmodulin-Dependent Protein Kinase |
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Authors: | Nobuhiro Inoue Takafumi Iwasa Kohji Fukunaga Yasuhiko Matsukado Eishichi Miyamoto |
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Institution: | Department of Neurosurgery, Kumamoto University Medical School, Kumamoto, Japan;Department of Pharmacology, Kumamoto University Medical School, Kumamoto, Japan |
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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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Keywords: | Multifunctional calmodulin-dependent protein kinase Glycogen synthase Brain |
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