Amino terminal sequences of mammalian Type C RNA tumor virus group-specific antigens

• Published in: Biochemical and biophysical research communications Vol. 48; no. 6; pp. 1549 - 1555
• Main Authors: Oroszlan, S., Copeland, T., Summers, M., Gilden, R.V.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.09.1972
• Subjects: Amino Acid Sequence; Animals; Antigens, Viral - analysis; Antigens, Viral - isolation & purification; Arginine - analysis; Autoanalysis; Cats; Chromatography, Gas; Chromatography, Gel; Chromatography, Thin Layer; Cross Reactions; Epitopes; Humans; Isoelectric Focusing; Leucine - analysis; Mice; Oncogenic Viruses - immunology; Proline - analysis; Retroviridae - immunology; RNA Viruses - immunology; Species Specificity; Viral Proteins - isolation & purification
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(72)90890-X

The amino terminal sequences of the major internal protein of three mammalian Type C viruses have been determined by automated and manual analyses. Individual residues were determined by gas chromatography, amino acid analyses, and thin layer chromatography. Fifteen positions were determined for mouse virus and three for cat and RD-114, the latter a candidate human virus. Proline and leucine were found at positions 1 and 2 of all three proteins; mouse and cat proteins contained arginine at position 3, while leucine was found at position 3 in RD-114 protein. These data strongly support the conclusion that these protein preparations which contain both species-specific and interspecific cross-reactive antigenic determinants consist of a single protein species. Further, the potential usefulness of sequence analysis for determination of relationships among Type C viruses is indicated.