The adenovirion has been shown to have a much more complex structure than was previously assumed. Eight different types of polypeptides have been assigned a place in the particle. Three are present in an outer capsid, three in an inner core, and two others in association with hexons. The hexon capsomere is composed of about three molecules of a single type of peptide of molecular weight (MW) 120,000 which comprises about 50% of the total virion protein. Groups of such capsomeres, released from the virion by 5 M urea, are found to be associated with two minor polypeptides, each of MW 13,000. The penton-base is composed of a single type of peptide of MW 70,000, and the fiber is composed of another peptide of MW 62,000. The internal core released by treatment of the virion with 5 M urea, contains the viral DNA in association with three arginine-rich peptides of MW 44,000, 24,000, and 24,000, comprising some 20% of the total virion protein. The same three peptides are relatively lacking in the "empty" capsids found as the "top components" of cesium chloride gradients of crude virus preparations.
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