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Abstract A purified rabbit skeletal muscle adenosine 3',5'-monophosphate (cyclic AMP)-stimulated protein kinase enhanced lipolytic activity in adipose tissue homogenates. This effect required the presence of cyclic AMP and ATP and was completely blocked by a protein inhibitor of cyclic AMP-stimulated protein kinases. It is inferred that this effect is due to the phosphorylation and activation of a lipase in a system analogous to that involved in the activation of muscle glycogen phosphorylase.
Corbin et al. (Tue,) studied this question.
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