Abstract
Isolated myosin light chain from chicken gizzard has been shown to serve as a substrate for Ca 2+-activated phospholipid-dependent protein kinase. Autoradiography showed that Ca 2+-activated phospholipid-dependent protein kinase phosphorylated mainly the 20,000-dalton light chain of chicken gizzard myosin. Exogenously added calmodulin had no effect on myosin light chain phosphorylation catalyzed by the enzyme. The 20,000-dalton myosin light chain, both in the isolated form and in the whole myosin form, served as the substrate for this enzyme. In contrast to the isolated myosin light chain, the light chain of whole myosin was phosphorylated to a lesser extent by the Ca 2+-activated phospholipid dependent kinase. Our results suggest the involvement of phospholipid in regulating Ca 2+-dependent phosphorylation of the 20,000-dalton light chain of smooth muscle myosin.
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