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- W1506704433 abstract "Poly(ADP-ribose) synthetase from bovine thymus was phosphorylated effectively by protein kinase C invitro. The phosphorylation was dependent on the activators of this kinase, Ca2+ and phospholipid. The apparent Km for the synthetase was about 8 μM, which was lower than that for histone H1. Though the synthetase was a weak substrate for Ca2+/calmodulin-dependent protein kinase II, other protein kinases, cyclic AMP-dependent and cofactor-independent protein kinases did not phosphorylate the synthetase. Phosphorylation of the synthetase by protein kinase C resulted in appreciable inhibition of the synthetase activity." @default.
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- W1506704433 date "1987-10-01" @default.
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- W1506704433 title "Poly(ADP-ribose) synthetase is phosphorylated by protein kinase C" @default.
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- W1506704433 doi "https://doi.org/10.1016/0006-291x(87)90934-x" @default.
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