Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-27923
Biochem Biophys Res Commun 1987 Oct 29;1482:709-17.
Show Gene links Show Anatomy links

Poly (ADP-ribose) synthetase is phosphorylated by protein kinase C in vitro.

Tanaka Y , Koide SS , Yoshihara K , Kamiya T .


???displayArticle.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.

???displayArticle.pubmedLink??? 3120711
???displayArticle.link??? Biochem Biophys Res Commun