Simian rotavirus (SA-11) isolated from infected African green monkey kidney cells was separated into two virus fractions in a CsCl density gradient and their proteins analysed on a continuous phosphate buffered polyacrylamide gel electrophoresis system. One peak (buoyant density 1.37 g/ml) contained double capsid virus particles which were radioimmunoassay (RIA)- and haemagglutinin (HA)-positive and yielded eight polypeptides whose mol. wt. ranged from 48000 to 128000. The second peak (buoyant density 1.39 g/ml) which contained 70% single capsid particles and was RIA-positive but HA-negative, yielded only five polypeptides. The three polypeptides missing in the second peak are associated presumably with the outer capsid of SA-11 virus particles and one or more of these is assumed to be the HA of SA-11 rotavirus.


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