Abstract
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. Mr 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.
Original language | English |
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Pages (from-to) | 5-11 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 148 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1 Nov 1982 |
Keywords
- Calmodulin
- Cyclic AMP
- Glycogen synthase
- Protein phosphorylation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology