Properties of a purified rat-liver nuclease.
1. The pH optimum, ionic requirement and heat-stability of a purified liver nuclease have been examined with RNA and denatured DNA as substrates. 2. The enzyme attacked DNA and RNA in an endonucleolytic manner, forming oligonucleotides terminated by 5'-phosphate groups. No clear specificity was found with respect to the bases at the site of cleavage. 3. Comparison of the results obtained with RNA and denatured DNA as substrates suggests that the ribonuclease and deoxyribonuclease activities are associated with the same protein.
D000818:Animals; D002845:Chromatography; D004247:DNA / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D012313:RNA / Q000378:metabolism*; D051381:Rats; D012260:Ribonucleases / Q000378:metabolism*
D008345:Manganese; D012313:RNA; D004247:DNA; D003851:Deoxyribonucleases; D012260:Ribonucleases; D008274:Magnesium