Purification and some properties of a deoxyribonucleic acid endonuclease endogenous to rat liver chromatin.
A deoxyribonucleic acid (DNA) endonucleolytic activity has been purified from a 0.3 M KCl extract of rat liver chromatin by a combination of selective precipitation and ion-exchange and gel filtration chromatography. The purified protein has a molecular weight of 35 000 as determined by Sephadex G-200 gel filtration and sodium dodecyl sulfate-acrylamide gel electrophoresis. The nuclease activity is stimulated by the addition of Mg2+ and thus may represent the Mg2+-activated DNase endogenous to chromatin. The purified enzyme has the ability to make both single-strand nicks and double-strand cuts in DNA.
D000818:Animals; D002413:Cations, Divalent; D002843:Chromatin / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D003850:Deoxyribonuclease I; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004720:Endonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004789:Enzyme Activation; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D013379:Substrate Specificity
D002413:Cations, Divalent; D002843:Chromatin; D003851:Deoxyribonucleases; D004720:Endonucleases; D003850:Deoxyribonuclease I