Published November 25, 1972
| public
Journal Article
Association of an Endorihonuclease with the Avian Myelohlastosis Virus Deoxyribonucleic Acid Polymerase
- Creators
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Baltimore, David
- Smoler, Donna F.
Abstract
A ribonuclease degrading only RNA complexed to DNA is found associated with the avian myeloblastosis virus DNA polymerase. A convenient and sensitive assay for the enzyme is degradation of [^3H]poly(A) complexed to poly(dT). Using this assay, nuclease and DNA polymerase activities are inseparable by DEAE-Sephadex or phosphocellulose ion exchange chromatography or by glycerol gradient centrifugation. Poly(A) labeled selectively at each end can be used to demonstrate that the nuclease is an endonuclease, and chromatography of the digestion products of poly(A) confirms this result. The oligonucleotide digestion products can be further digested to 5'-AMP by venom phosphodiesterase, indicating that they are terminated by 3'-OH groups
Additional Information
© 1972 American Society of Biological Chemists. Received for publication, June 9, 1972. This work was supported by a grant from the American Cancer Society and a contract from the Special Virus Cancer Program of the National Cancer Institute. Faculty Hesearch Awardee of the American Cancer Society. F. J. Bollum, personal communication. We are grateful for the advice and assistance of Drs. I. Molineux, U. L. RajBhandary, and I. Verma.Additional details
- Eprint ID
- 32688
- Resolver ID
- CaltechAUTHORS:20120724-145350321
- American Cancer Society
- National Cancer Institute Special Virus Cancer Program
- Created
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2012-07-24Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field