Published November 25, 1972 | Version public
Journal Article

Association of an Endorihonuclease with the Avian Myelohlastosis Virus Deoxyribonucleic Acid Polymerase

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

Identifiers

Eprint ID
32688
Resolver ID
CaltechAUTHORS:20120724-145350321

Funding

American Cancer Society
National Cancer Institute Special Virus Cancer Program

Dates

Created
2012-07-24
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Updated
2019-10-03
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