Abstract
The 30,000-molecular-weight internal protein, p30, was purified from seven strains of mouse type-C viruses. The individual p30's showed variation in isoelectric points and also intrastrain heterogeneity. The individual p30's could be distinguished by peptide map and quantitative complement fixation techniques with relatedness estimates of >95%. Amino terminal sequence analysis showed variability at position 4 for several p30's with complete homology otherwise through 24 residues. The intrastrain heterogeneity in p30 isoelectric points could not be explained by common contaminants, as shown by peptide mapping, and is more likely based on post-transcriptional modifications. These data provide a chemical basis for the recently described type-specific immunological properties of individual p30's.