Tang, David (1978) Purification of a DNA nicking-closing enzyme from mouse L cells. Nucleic Acids Research, 5 (8). pp. 2861-2875. ISSN 0305-1048 http://resolver.caltech.edu/CaltechAUTHORS:TANnar78
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Abstract
A DNA nicking-closing enzyme has been purified from the nuclei of souse L cells to 90% homogeneity. The denatured and reduced form of the enzyme has a molecular weight of 68,000 which is In agreement with the molecular weight of the native enzyme as determined by gel filtration and by sucrose sedimentation velocity assuming the protein is globular. Therefore, the active form of the enzyme is a monopolypeptide. Its isoelectric. point is pH 4.2 ± 0.2. The nicking-closing activity does not require a cofactor arid does not involve any sulfhydryl group. The enzyme requires 0.2 M NaCl and pH in the range of 6.5–7.5 for optimal activity.
| Item Type: | Article |
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| Additional Information: | Copyright © 1978 Oxford University Press. Received April 20, 1978. This work was supported by Grants CA 08014 and GM 15327 from the United States Public Health Service to Dr. Jerome Vinograd. Thanks are due to Judith Campbell, Norman Davidson, and Tom Maniatis for their critical review of the mauscript. |
| Record Number: | CaltechAUTHORS:TANnar78 |
| Persistent URL: | http://resolver.caltech.edu/CaltechAUTHORS:TANnar78 |
| Alternative URL: | http://nar.oxfordjournals.org/cgi/content/abstract/5/8/2861 |
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. |
| ID Code: | 4052 |
| Collection: | CaltechAUTHORS |
| Deposited By: | Tony Diaz |
| Deposited On: | 25 Jul 2006 |
| Last Modified: | 26 Dec 2012 08:57 |
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