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...
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Published in | Biochemistry (Easton) Vol. 20; no. 19; pp. 5466 - 5470 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
15.09.1981
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Subjects | |
Online Access | Get full text |
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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. |
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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 |