Abstract
The regulation of phosphorylase kinase has been studied in crude homogenates of adult flies and larval brains of Drosophila melanogaster. The kinase has an alkaline pH optimum (about pH 8.6), is inhibited by an excess of Mg 2+ and is stimulated by Ca 2+ in the homogenates. Incubation of larval brains with octopamine, especially in the presence of theophylline, or with forskolin, markedly elevated the level of cAMP with no, or marginal, activation of phosphorylase. In contrast, Ca 2+ in the presence of A-23187 caused a two-fold increase in phosphorylase a. The mutant dunce M11 flies contain six to seven times as much cAMP as the wild type Canton-S flies and have a somewhat elevated phosphorylase a level.
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