Poly(ADP-ribose) polymerase from Ehrlich ascites-tumour cells. Amino acid composition, N-terminal analysis and chemical cleavage of the purified protein.
Poly(ADP-ribose) polymerase was purified from Ehrlich ascites-tumour cells by two novel methods. Analysis for amino acid composition revealed a high percentage of acidic amino acids or their amides, and of basic amino acids. N-Terminal analysis with dansyl chloride revealed no terminal amino acid, indicating a blocked N-terminal amino group. Analysis by gel electrophoresis of protein treated with 3-bromo-3-methyl-2-[(2-nitrophenylthio)-3H-indole, under conditions where selective cleavage of the polypeptide chain at tryptophan residues is obtained, showed six major peptide bands.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D009244:NAD+ Nucleosidase / Q000302:isolation & purification; D011065:Poly(ADP-ribose) Polymerases / Q000302:isolation & purification; D012862:Skatole / Q000031:analogs & derivatives
D000596:Amino Acids; C005904:BNPS-skatole; D012862:Skatole; D011065:Poly(ADP-ribose) Polymerases; D009244:NAD+ Nucleosidase