Ribonucleases protect RNA from acid precipitation.
Four, widely used, ribonucleases were found to protect their substrates from acid precipitation by causing, evidently, a modification of their physicochemical properties. The protection was dependent on the kind of substrate while the ratio of protective to nucleolytic activity varied widely between the four enzymes. The protection was enhanced by some nucleotides like UMP, CMP and IMP and decreased in the presence of several bivalent ions like Zn++, Co++ and Cu++. It was completely abolished when the substrates were hybridized with their complementary ribohomopolymers. In the case of bovine pancreatic ribonuclease, the part of the molecule which was responsible for the protective activity was localized on the enzyme domain characterized as S-protein, which lacks nucleolytic activity. The observed property of ribonucleases could lead to false data when the measurement of TCA-soluble material is the method used to follow the purification of ribonucleases or to study their activity. It was also found that ribonuclease S-protein enhances the catalytic activity of B. Cereus RNAse. S-protein could potentiate other RNAses activity like onconase, which has recently been used as an anticancer agent.
Kouretas
D
D
Laboratory of Pharmacology, School of Veterinary Medicine, University of Thessaly, Karditsa, Greece.
Antonoglou
O
O
D000143:Acids / Q000378:metabolism; D011232:Chemical Precipitation; D003035:Cobalt / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D009705:Nucleosides / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism
D000143:Acids; D009705:Nucleosides; D003035:Cobalt; D012313:RNA; D003300:Copper; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic; D015032:Zinc