Abstract
1. 1. Two types of myosins with phosphorylated and dephosphorylated myosin light chains were prepared from Drosophila flies. The former had ATPase ( Ca 2+- and Mg 2+-activated ) activities twice those of the latter. 2. 2. The myosin phosphorylated with crude myosin light chain kinase from flies showed ATPase ( Ca 2+- and Mg 2+-activated ) activaties twice those of the dephosphorylated myosin. 3. 3. It is suggested that phosphorylation of myosin light chains several hours after emergence stimulates myosin ATPase activity so as to facilitate the flight function of the fruitfly.
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