Lai, M. M.C., Neil, J. C. and Vogt, P. K. (1980) Cell-free translation of avian erythroblastosis virus RNA yields two specific and distinct proteins with molecular weights of 75,000 and 40,000. Virology, 100(2), pp. 475-483. (doi: 10.1016/0042-6822(80)90537-1) (PMID:6243437)
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Abstract
Avian erythroblastosis virus (AEV) 28 S virion RNA was translated in vitro in cell-free reticulocyte lysates. Two AEV-specific proteins, one of 75,000 (p75) the other of 40,000 (p40) molecular weight, were detected. p75 is a fusion protein containing gag-specific and AEV-specific peptides. It appears to be translated from the 5′-end of the 28 S AEV RNA and is indistinguishable from the p75 detected in AEV-transformed cells (Hayman et al., 1979). p40 does not share sequences with any viral structural protein. It also contains peptides distinct from those of p75, but one of the five identifiable p40 peptides comigrates with one of the p75 peptides. p40 is translated from a 20 S RNA which contains the 3′-half of the AEV-specific sequences of the genome. These two proteins account for all of the coding capacity of the AEV-specific gene sequences in the 28 S AEV RNA and are candidates for leukemia-specific transforming proteins.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Neil, Professor James |
| Authors: | Lai, M. M.C., Neil, J. C., and Vogt, P. K. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity |
| Journal Name: | Virology |
| Publisher: | Elsevier |
| ISSN: | 0042-6822 |
| ISSN (Online): | 1096-0341 |
| Published Online: | 23 February 2004 |
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