Purification and some properties of a nuclease from rye germ nuclei.
1. An endonuclease has been isolated from the nuclei of rye (Secale cereale L) germ and partially purified. The enzyme shows optimum activity over the pH range 5.4-7.4 towards both DNA and RNA, and has no phosphomonoesterase or phosphodiesterase activity. 2. DNA is degraded by the rye germ nuclease to oligonucleotides of similar size, and RNA to oligonucleotides and mononucleotides containing a C-terminal 5'-phosphate group. 3. The rate of hydrolysis of nuclear acids by the enzyme decreases in the following order: native DNA greater than denatured DNA greater than RNA. Synthetic polynucleotides are hydrolysed at a rate decreasing in the order: poly(A) greater than poly(U) greater than poly(C) greater than poly(G).
D002467:Cell Nucleus / Q000201:enzymology*; D002845:Chromatography; D003851:Deoxyribonucleases / Q000302:isolation & purification*; D002523:Edible Grain / Q000201:enzymology*; D006868:Hydrolysis; D008970:Molecular Weight; D012260:Ribonucleases / Q000302:isolation & purification*; D012434:Secale / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology*
D003851:Deoxyribonucleases; D012260:Ribonucleases