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Glycogen phosphorylase (GP) is an enzyme that catalyzes the transfer of phosphate from phosphorylase a to glycogen. The enzyme activity is regulated by several calcium-binding proteins. The glycogen phosphorylase activity in guinea pig brain was partially purified by DEAE-cellulose chromatography. There was no difference in the GP activity between the microsomal fraction of guinea pig brain and the purified enzyme. When the purified enzyme was incubated with [gamma-32P]ATP, the C-terminal phosphorylation site (GS) of glycogen synthase was identified. The GP activity was stimulated by the presence of 0.1 mg/ml phosphodiesterase inhibitors, isobutylmethylxanthine, theophylline, and the divalent cation, Mg2+ or Ca2+, indicating that the phosphodiesterase inhibitors may cause an increase in the intracellular level of cAMP. It was found that calcium-channel blockers, verapamil, nifedipine, and diltiazem, inhibited the GP activity in a concentration-dependent manner with IC50 values of 0.3, 0.5, and 4.0 microM, respectively. On the other hand, the effects of nifedipine and diltiazem were blocked by the addition of nifedipine and diltiazem to the reaction mixture, respectively. The effect of diltiazem was not affected by the prior addition of calcium ion. All three calcium-channel blockers inhibited the phosphodiesterase activity of brain microsomes in a concentration-dependent manner, with IC50 values of 0.4, 0.6, and 0.3 microM for verapamil, nifedipine, and diltiazem, respectively. These results indicate that the GP activity

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