A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.
ASJC Scopus subject areas
- Molecular Biology