1. Reversible inactivation of ribonucleases by ADPribosylation.
- Author
-
Leone E, Farina B, and Faraone Mennella MR
- Subjects
- Adenosine Diphosphate Ribose pharmacology, Animals, Cattle, Cell Nucleus enzymology, Hydrolysis, Kinetics, Male, NAD metabolism, Nucleotidyltransferases metabolism, Poly(ADP-ribose) Polymerases, Ribonuclease, Pancreatic antagonists & inhibitors, Ribonuclease, Pancreatic metabolism, Ribonucleases metabolism, Semen enzymology, Spectrophotometry, Ultraviolet, Adenosine Diphosphate Ribose metabolism, Nucleoside Diphosphate Sugars metabolism, Ribonucleases antagonists & inhibitors
- Abstract
The activity of purified bovine seminal RNAase and pancreatic RNAase A (EC 3.1.27.5) has been investigated following in vitro ADPribosylation in the presence of nuclear ADPribosyltransferase (EC 2.4.2.30) and NAD+ X ADPribosylation of these enzymes was correlated with a significant decrease in their activities. Approximately three residues of ADPribose were present per mol of enzyme. Removal of the bound ADPribose restored enzyme activity to near normal levels. Similar results were obtained with nuclei isolated from bull seminal vesicles as an endogenous source of seminal RNAase and nuclear ADPribosyltransferase. The findings suggest that in vitro ADPribosylation has a reversible inactivating effect on ribonucleases.
- Published
- 1986
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