Identification of a calmodulin‐dependent glycogen synthase kinase in rabbit skeletal muscle, distinct from phosphorylase kinase
JR Woodgett, NK Tonks, P Cohen - FEBS letters, 1982 - Wiley Online Library
JR Woodgett, NK Tonks, P Cohen
FEBS letters, 1982•Wiley Online LibraryA glycogen synthase kinase that is completely dependent on Ca2+ and calmodulin has
been identified in mammalian skeletal muscle, and purified∼ 3000‐fold by chromatography
on phosphocellulose and calmodulin—Sepharose. The presence of 50 mM NaCl in the
homogenisation buffer was critical for extraction of the enzyme. The calmodulin‐dependent
glycogen synthase kinase (app. M r 850 000) is distinct from myosin light‐chain kinase and
phosphorylase kinase, but phosphorylates the same serine residue on glycogen synthase …
been identified in mammalian skeletal muscle, and purified∼ 3000‐fold by chromatography
on phosphocellulose and calmodulin—Sepharose. The presence of 50 mM NaCl in the
homogenisation buffer was critical for extraction of the enzyme. The calmodulin‐dependent
glycogen synthase kinase (app. M r 850 000) is distinct from myosin light‐chain kinase and
phosphorylase kinase, but phosphorylates the same serine residue on glycogen synthase …
A glycogen synthase kinase that is completely dependent on Ca2+ and calmodulin has been identified in mammalian skeletal muscle, and purified ∼3000‐fold by chromatography on phosphocellulose and calmodulin—Sepharose. The presence of 50 mM NaCl in the homogenisation buffer was critical for extraction of the enzyme. The calmodulin‐dependent glycogen synthase kinase (app. M r 850 000) is distinct from myosin light‐chain kinase and phosphorylase kinase, but phosphorylates the same serine residue on glycogen synthase as phosphorylase kinase. The physiological role of the enzyme is discussed.
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