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Ca 2+ , calmodulin‐dependent phosphorylation of glycogen synthase by a brain protein kinase
Author(s) -
Iwasa Takafumi,
Fukunaga Kohji,
Yamamoto Hideyuki,
Tanaka Etsuro,
Miyamoto Eishichi
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80723-6
Subject(s) - glycogen synthase , phosphorylation , biochemistry , calmodulin , gsk 3 , chemistry , cyanogen bromide , glycogen phosphorylase , phosphorylase kinase , glycogen branching enzyme , trifluoperazine , protein kinase a , egta , gsk3b , glycogen , protein phosphorylation , enzyme , microbiology and biotechnology , biology , calcium , peptide sequence , organic chemistry , gene
A Ca 2+ , calmodulin‐dependent protein kinase from brain with a M r of 640 000 is capable of phosphorylating glycogen synthase from skeletal muscle. The reaction was inhibited by the addition of 1 mM EGTA and 50 μM trifluoperazine, but not by protein kinase inhibitor and heparin. The amount of phosphate incorporated into glycogen synthase was 1.4 mol/mol subunit. The phosphorylation sites of glycogen synthase were cyanogen bromide‐treated peptides CB‐1 and CB‐2 and only the seryl residue was phosphorylated.