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- W1967479968 abstract "A calmodulin-dependent protein kinase from canine myocardial cytosol was purified 1150-fold to apparent homogeneity with a 1.5% yield. The purified enzyme had a Mr of 550,000 with a sedimentation coefficient of 16.6 S, and showed a single protein band with a Mr of 55,000 (55K protein), determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme had a specific activity of 1.6 μmol/mg protein/min, and Ka values of 67 nM and 1.1 μM for calmodulin and Ca2+, respectively, using chicken gizzard myosin light chain as substrate. Calmodulin bound to the 55K protein. The purified enzyme had a broad substrate specificity. Endogenous proteins including glycogen synthase, phospholamban, and troponin I from the canine heart were phosphorylated by the enzyme. These results suggest that the purified enzyme works as a multifunctional protein kinase in the Ca2+, calmodulin-dependent cellular functions of the canine myocardium, and that the enzyme resembles enzymes detected in the brain, liver, and skeletal muscle." @default.
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- W1967479968 date "1986-07-01" @default.
- W1967479968 modified "2023-10-12" @default.
- W1967479968 title "Purification and characterization of a multifunctional calmodulin-dependent protein kinase from canine myocardial cytosol" @default.
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- W1967479968 doi "https://doi.org/10.1016/0003-9861(86)90396-6" @default.
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