Disk electrophoresis in polyacrylamide gel was used to study the polypeptide composition of purified virions of simian adenoviruses SA7, SV20 (H), and SV 38 as well as human adenovirus type 6. The general electrophoretic pattern of separation of structural polypeptides of simian and human adenoviruses was shown to be similar; the role of a number of components in the virion was elucidated. All the simian adenoviruses under study were found to have the following characteristic sizes of polypeptide components: components V and VII (DNA-framework) 50-51 and 18-19 kilodaltons, respectively, polypeptide VI (prihexon component) 29-30 kilodaltons. Simian adenovirions differ from all human adenovirus serotypes studied in the size of component VI. Capsid components (polypeptides II, III, and IV) vary in size in individual serotypes of simian adenoviruses, their set being unique for each serotype and allowing to distinguish simian adenoviruses by their electrophoretic patterns.
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