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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| 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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| AbstractList | 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. 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 Mg super(2+) and thus may represent the Mg super(2+)-activated DNase endogenous to chromatin. The purified enzyme has the ability to make both single-strand nicks and double-strand cuts in DNA. |
| Author | Machray, Gordon C Bonner, James |
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| SubjectTerms | 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 |
| Title | Purification and some properties of a deoxyribonucleic acid endonuclease endogenous to rat liver chromatin |
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