Harter, M. L., Lewis, J. B., Anderson, C. W. (September 1979) Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteins. J Virol, 31 (3). pp. 823-35. ISSN 0022-538X (Print)0022-538X (Linking)
Abstract
The protein covalently bound to the 5' termini of adenovirus type 2 DNA has been purified from virus labeled with [35S]methionine, using exclusion chromatography of disrupted virions to isolate the DNA-protein complex, which is then digested with DNase. The terminal protein isolated from mature virus is most effectively labeled if the cells are exposed to [35S]methionine during the "intermediate" period of 13 to 21 h postinfection, suggesting that the protein is synthesized during this interval. The tryptic peptides of the terminal protein were compared with those of several known adenovirus-coded proteins and found to be unrelated. In particular, the terminal protein is not related to the 38-50K early proteins encoded by the leftmost 4.4% of the adenovirus genome, one region essential for the transforming activity of the virus. Neither is it related to the 72K single-strand-specific DNA binding protein, the minor virion component IVa2, or the major capsid component hexon.
Item Type: | Paper |
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Uncontrolled Keywords: | Adenoviruses, Human/*analysis/metabolism DNA, Viral/isolation & purification/metabolism HeLa Cells Humans Peptides/analysis Trypsin Viral Proteins/analysis/biosynthesis/*isolation & purification |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification organism description > virus > adenovirus |
CSHL Authors: | |
Communities: | CSHL labs |
Depositing User: | Matt Covey |
Date: | September 1979 |
Date Deposited: | 25 May 2016 15:42 |
Last Modified: | 25 May 2016 15:42 |
PMCID: | PMC353510 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32690 |
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