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-2...

Full description

Saved in:
Bibliographic Details
Published inBiochemistry (Easton) Vol. 20; no. 19; pp. 5466 - 5470
Main Authors Machray, Gordon C, Bonner, James
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 15.09.1981
Subjects
Animals
Cations, Divalent
chromatin
Chromatin - enzymology
Chromatography, Ion Exchange
Deoxyribonuclease I
Deoxyribonucleases - isolation & purification
Deoxyribonucleases - metabolism
endodeoxyribonuclease
Endonucleases - isolation & purification
Endonucleases - metabolism
Enzyme Activation
Kinetics
liver
Liver - enzymology
Molecular Weight
purification
Rats
Substrate Specificity
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:istex:5921AB523CEF7C6C0202A8F99F35DD3B5D448AD4
ark:/67375/TPS-XNV5RW1Z-5
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00522a018