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Biochemical study demonstrates cyclic AMP-dependent protein kinase activity in rabbit skeletal muscle, highlighting its role in activating phosphorylase kinase.
A protein kinase that catalyzes an adenosine 3',5'-monophosphate (cyclic AMP)-dependent phosphorylation of casein and protamine has been purified from rabbit skeletal muscle. The Km values of cyclic AMP for these reactions are 1 x 10-7 and 6 x 10-8 m, respectively. The protein kinase markedly increases the rate of the cyclic AMP-dependent activation and phosphorylation of phosphorylase kinase by ATP.
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Walsh et al. (1968) studied this question.
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