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Structural Heterogeneity in p30 Molecules of Type C Viruses

Robert C. Mellors

The Hospital for Special Surgery Affiliated with the New York Hospital-Cornell University Medical College, New York, N.Y., U.S.A.

Tryptic digests of p30 proteins from mouse type C viruses were subjected to cation-exchange chromatography. Structural heterogeneity of p30 molecules was seen in two specific areas of the peptide elution profiles. These hypervariable regions of p30 proteins were used to discriminate representative ecotropic (N- and B-tropic), xenotropic (alpha and beta) and amphotropic viruses.

^* Present address: Sloan-Kettering Institute, New York, N.Y., U.S.A.

To whom reprint requests should be addressed.

Received 25 September 1979; accepted 15 February 1980.