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

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Abstract
The protein covalently bound to the 5'' germini of adenovirus type 2 DNA was 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 13-21 h post-infection, 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 were unrelated. The terminal protein is not related to the 38-50K [38,000-50,000 dalton] early proteins encoded by the leftmost 4.4% of the adenovirus genome, 1 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.