Occurrence of a nucleoprotein bound RNase in rat brain and liver.
An RNase activity was found to be present in rat brain and liver and was strongly bound to the nucleoprotein fractions of these tissues. It could not be solubilized by treatment with acid or by lipid solvents. The pattern of oligonucleotides produced during hydrolysis by this enzyme indicated that it was probably an endonuclease with restricted specificity. It was inhibited by zinc ions and by low pH.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D008297:Male; D009698:Nucleoproteins / Q000378:metabolism*; D009841:Oligonucleotides / Q000378:metabolism; D012331:RNA, Fungal / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D006163:Ribonuclease T1 / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D013379:Substrate Specificity
D009698:Nucleoproteins; D009841:Oligonucleotides; D012331:RNA, Fungal; D012260:Ribonucleases; D006163:Ribonuclease T1; D012259:Ribonuclease, Pancreatic