title: Studies on sheep kidney nuclease. I. An improved purification method and some properties.
abstract: An improved purification method of the sheep kidney nuclease (nuclease SK) specific for single-strans nucleic acid, which includes extraction with 0.85% NaCl, treatment with DEAE-cellulose, fractionation with polyethylene glycol, phospho-cellulose chromatography, CM-Sephadex chromatography and phospho-cellulose rechromatography is described. The nuclease was purified approx. 390-fold. Identity was established by comparison with known properties. Molecular weight was estimated to be 52 000-53 000 by gel filtration on Sephadex G-100. The properties of the purified enzyme agreed well those reported previously. The purified enzyme hydrolyzed heat-denatured calf thymus DNA, yeast RNA and no hydrolytic activity for native calf thymus DNA, A2'-pA, A3'-pA, ADP, ATP, 5'-AMP and cyclic AMP.
mesh_terms: D000818:Animals; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism; D004720:Endonucleases / Q000302:isolation & purification / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008970:Molecular Weight; D012260:Ribonucleases / Q000302:isolation & purification / Q000378:metabolism; D012756:Sheep; D013379:Substrate Specificity
chemical_list: D002729:Chloromercuribenzoates; D003851:Deoxyribonucleases; D004720:Endonucleases; D012260:Ribonucleases; C021886:nuclease SK