Activation of Glycogen Phosphorylase by Cyclic AMP in <i>Tetrahymena pyriformis</i>1

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<jats:title>ABSTRACT</jats:title><jats:p>Glycogen phosphorylase in <jats:italic>Tetrahymena pyriformis</jats:italic> was activated by a Mg<jats:sup>2+</jats:sup> ATP‐dependent process and this activation was further increased by the addition of cyclic AMP. When the enzyme activity in subcellular fractions was measured, it was largely associated with the glycogen fraction but was no longer activated by ATP and cyclic AMP. Mixing the glycogen fraction and cytosol fraction together restored the effects of ATP and cyclic AMP on phosphorylase activity. These findings suggest that glycogen phosphorylase associated with <jats:italic>Tetrahymena</jats:italic> glycogen granules may be regulated by cytosolic factor(s) with cyclic AMP.</jats:p>

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