Abstract
Methylxanthines interact with the cyclic nucleotide-dependent phosphorylation of proteins; they are potent inhibitors of cyclic nucleotide phosphodiesterase from human and animal tissues [l]: such that they increase CAMP level and indirectly stimulate CAMP-dependent phosphorylation. In studies on phosphorylation of the red blood cell proteins we observed that methylxanthine derivatives inhibited CAMP-independent phosphorylation. Here, we show that two methylxanthine derivatives, caffeine and pentoxifylline (3,7dimethyl 1-(5-0x0hexyl) xanthine) are inhibitors of a purified casein kinase from human red cell and that they act as competitive inhibitors for the ATP binding site of enzyme.
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