The mouse Lyt-2/3 antigen complex--II. Structural analysis of the subunits.
Surface- or biosynthetically labeled Lyt-2/3 antigens were isolated from cell lysates by immunoprecipitation and affinity chromatography with a monoclonal antibody. Tryptic digests of the individual subunits of 37,000, 32,000 and 28,000 apparent mol. wts were analysed by reverse-phase high-performance liquid chromatography and by two-dimensional peptide mapping. The results indicate that the 37,000 and 32,000 mol. wt components are structurally very similar whereas the 28,000 mol. wt component appears as a different molecule.
D000818:Animals; D000950:Antigens, Ly; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D005260:Female; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000950:Antigens, Ly; D010446:Peptide Fragments; D014357:Trypsin