Preferential ADP-ribosylation of arginine-3 in synthetic heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly.
Hen liver nuclear ADP-ribosyltransferase modified the synthetic heptapeptide Kemptide (Leu-Arg-Arg-Ala-Ser-Leu-Gly) at arginine-2 and/or arginine-3. Trypsin treatment of ADP-ribosyl-Kemptide revealed that the ADP-ribosylation of arginine-3 was constantly more abundant than that of arginine-2. ADP-ribosylation of Kemptide suppressed the subsequent phosphorylation by cyclic AMP-dependent protein kinase.
D000244:Adenosine Diphosphate / Q000378:metabolism*; D001120:Arginine / Q000032:analysis; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D009842:Oligopeptides / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism
D009842:Oligopeptides; D010446:Peptide Fragments; D000244:Adenosine Diphosphate; C037642:kemptide; D001120:Arginine; D011065:Poly(ADP-ribose) Polymerases