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- W2007677360 abstract "Abstract Highly purified polyoma virus particles contain four nonhistone polypeptides. Their approximate molecular weights are 86,000 (VP0), 48,000 (VP1), 35,000 (VP2), and 23,000 (VP3). These polypeptides have been isolated by SDS-polyacrylamide-gel electrophoresis. The primary structure of the various differentially labelled (14C]- or [3H]lysine plus arginine) polypeptides were compared by an analysis of their tryptic peptides by use of ion-exchange and paper chromatography. The results indicate that VP0 and VP1 have identical peptide maps and that VP0 is probably a dimer of VP1. All of the tryptic peptides derived from VP3 were also detected in the tryptic digest of VP2. Additional peptides that were found in the VP2 digest and not in the VP3 appears to be derived from VP2. Whether this is of biological significance is not known. VP1 shares very few, if any, tryptic peptides with VP2 and VP3. These results are consistent with there being two polyoma genes coding for the virion proteins. One gene codes for VP1 and the other for VP2." @default.
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- W2007677360 date "1975-08-01" @default.
- W2007677360 modified "2023-09-25" @default.
- W2007677360 title "Nonhistone virion proteins of polyoma: Characterisation of the particle proteins by tryptic peptide analysis by use of ion-exchange columns" @default.
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- W2007677360 doi "https://doi.org/10.1016/0042-6822(75)90213-5" @default.
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