Abstract
The polypeptide composition of labeled BK virus was compared with that of simian virus 40 (SV40) and polyoma virus by co-electrophoresis of disrupted virions in polyacrylamide gels containing approximately 73% of the capsid protein and had a molecular weight of 39,000. It was smaller than VP1 of SV40 and polyoma virus. The other polypeptides of BK virus were similar in molecular weight to those of SV40. A comparison of the proteins of BK virus and SV40 iodinated with chloramine T before and after disruption in alkaline buffer at pH 10.5 revealed differences between the two viruses in the number and distribution of tyrosines available for iodination. The tryptic peptides of VP1, VP3, VP4, and VP5 combined of SV40 were compared with those of the same polypeptides of BK virus. Among the 19 peptides of VP1 resolved, only two were common to both viruses. The analyses of VP4 and VP5, the histone-like proteins, however, showed more similarity between the viruses, with 6 of 15 resolved peptides in common. The tryptic digests of VP3 were completely different.
MeSH Terms
Carbon Radioisotopes
Centrifugation, Zonal
Electrophoresis, Polyacrylamide Gel
Iodine
Lysine
Molecular Weight
Papillomaviridae/analysis
Peptides/analysis
Polyomaviridae
Polyomavirus/analysis
Protein Hydrolysates
Simian virus 40/analysis
Tritium
Trypsin
Chemicals
Carbon Radioisotopes
Peptides
Protein Hydrolysates
Tritium
Iodine
Trypsin
Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wright P J
Di Mayorca G
References (21)
21 references, click to expand
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