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  • Title: Poly (ADP-ribose) synthetase is phosphorylated by protein kinase C in vitro.
    Author: Tanaka Y, Koide SS, Yoshihara K, Kamiya T.
    Journal: Biochem Biophys Res Commun; 1987 Oct 29; 148(2):709-17. PubMed ID: 3120711.
    Abstract:
    Poly (ADP-ribose) synthetase from bovine thymus was phosphorylated effectively by protein kinase C in vitro. The phosphorylation was dependent on the activators of this kinase, Ca2+ and phospholipid. The apparent Km for the synthetase was about 8 microM, 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.
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