Abstract
Summary Cytoplasmic extracts from poliovirus type 1-infected HeLa cells labelled with 35 S-methionine 3 to 4 h after infection were analysed by sucrose gradient centrifugation, followed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Capsid proteins VP0, VP1 and VP3 were readily detected at 5S (monomeric capsomers) and at 14S (pentamers), whereas capsid precursor polypeptide 1a was detected mainly in a peak at 8S. No capsid polypeptide could be detected sedimenting freely at the top of the gradient. Immunoprecipitation of the labelled material using antibodies raised against individual virus capsid polypeptides showed that all three capsid polypeptides were immunoprecipitated together by either anti-VP1, anti-VP2 or anti-VP3 antisera, suggesting that the polypeptides were not free in the extract, but rather, were maintained in close physical association as the three polypeptide chains of a single capsid protein.
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