Detection of adenosine diphosphate-ribosyl transferase activity in the filarial worm, Onchocerca volvulus.
The existence of the nuclear enzyme ADP-ribosyl transferase in the filarial worm Onchocerca volvulus was demonstrated. The enzyme activity was observed in the nuclear preparation from the parasitic organism. Poly(ADP-ribose) was identified as the reaction product by the isolation of phosphoribosyl-AMP and 5'AMP as the major products of snake-venom phosphodiesterase digestion. The temperature and pH optima for the enzyme were 25 degrees C and 8.5, respectively. The apparent Km value exhibited by the substrate NAD+, is 750 microM and the activity of the enzyme is inhibited by four chemical classes of inhibitors, nicotinamides, methylxanthines, thymidine and aromatic amides.
D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009854:Onchocerca / Q000201:enzymology*; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D013696:Temperature
D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D011065:Poly(ADP-ribose) Polymerases