Spontaneous and Tryptic Degradation of Virus Particles and Structural Components of Adenoviruses

SUMMARY Electrophoretic analyses of the polypeptide components of adenovirus indicate that both the hexon and the penton base are degraded during storage of either purified virus preparations or isolated antigens. These two protein components are also degraded by trypsin and the products of tryptic digestion of native hexons were examined in detail. They were shown to consist of six polypeptide species which may result from tryptic action at three distinct sites on the hexon polypeptide. Both spontaneously degraded and trypsinized hexon and penton base proteins retained their morphological and antigenic characteristics.