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. 1981 Sep 15;20(19):5466-70.
doi: 10.1021/bi00522a018.

Purification and some properties of a deoxyribonucleic acid endonuclease endogenous to rat liver chromatin

G C Machray, J Bonner

Purification and some properties of a deoxyribonucleic acid endonuclease endogenous to rat liver chromatin

G C Machray et al. Biochemistry. .

Abstract

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.

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