Structural heterogeneity in p30 molecules of type C viruses.
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.
D000818:Animals; D002852:Chromatography, Ion Exchange; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D008814:Mice, Inbred NZB; D010802:Phylogeny; D012190:Retroviridae / Q000032:analysis* / Q000145:classification; D014764:Viral Proteins / Q000302:isolation & purification*
D014764:Viral Proteins