Abstract

The major internal protein, p30, of mammalian Type C viruses contains multiple antigenic determinants in both species-specific and interspecific categories. These were demonstrated by use of p30s modified reversibly by citraconylation, and a p30 fragment isolated after limited trypsin digestion. Six distinct reactivities were demonstrated by direct and absorption analyses in gel diffusion. In certain instances, separation of distinct antibody populations was also achieved by use of immunoadsorbents. Citraconylated p30 (p30c) was deficient in two of three species-specific reactivities, and at least one of three interspecies reactivities. A tryptic fragment from mouse p30 contained one species-specific determinant not shared with p30c and lacked one interspecies determinant contained in p30c. P30c also contained a species-specific determinant not shared with the tryptic fragment.

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