ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria.
ADP-ribosyl transferase and NAD glycohydrolase activities have been estimated in mitochondria in mitoplasts as well as in other submitochondrial fractions. A high activity of these two enzymes was present in mitoplasts as compared to the outer membrane preparation or intermembrane compartment. Inhibitor studies provide strong evidence for the involvement of ADP-ribosyl transferase in the process of ADP-ribosylation of mitochondrial proteins. When NAD glycohydrolase was blocked by nicotinamide or 3-aminobenzamide, the incorporation of ADP-ribose into mitochondrial proteins still occurs. ADP-ribosyl transferase activity could also be detected when NAD glycohydrolase was separated by hydroxylapatite chromatography. The protein-linked ADP-ribose moiety appears to be an oligomer in mitochondria.
D000818:Animals; D007425:Intracellular Membranes / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009244:NAD+ Nucleosidase / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013367:Submitochondrial Particles / Q000201:enzymology
D011065:Poly(ADP-ribose) Polymerases; D009244:NAD+ Nucleosidase