Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteins

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)

URL: http://www.ncbi.nlm.nih.gov/pubmed/513195

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
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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