Nucleoside diphosphokinase activity associated with DNA polymerases
- Creators
- Miller, Lois K.
- Wells, Robert D.
Abstract
Nucleoside diphosphokinase activity is present in highly purified preparations of DNA polymerase from Micrococcus luteus and Escherichia coli, and in a partially purified DNA polymerase from avian myeloblastosis virus. The activity is also observed in the protein fragment of molecular weight 76,000 that is produced by subtilisin cleavage of DNA polymerase I from E. coli. The NDP kinase activity in DNA polymerase preparations from M. luteus uses various ribo- and deoxyribonucleoside di- and triphosphates as substrates. The presence of this activity in preparations of DNA polymerase results in the apparent use of deoxyribonucleoside diphosphates as substrates for DNA synthesis, provided that some triphosphate is present to serve as a phosphate donor.
Additional Information
© 1971 by the National Academy of Sciences. Communicated by Henry A. Lardy, June 23, 1971. This work was supported by the National Science Foundation (GB-8786), the National Institutes of Health (NIH-71-2275), and the Jane Coffin Childs Memorial Fund. L.K.M. was a Woodrow Wilson Fellow and a predoctoral trainee of the National Institute of General Medical Science (GM 00236 BCH).Files
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Additional details
- Eprint ID
- 8091
- Resolver ID
- CaltechAUTHORS:MILpnas71
- Created
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2007-07-30Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field