Tryptic peptide disparity between serologically indistinguishable guinea pig Ia.3,5 antigens.

Serological studies have suggested that the DHCBA strain guinea pig expresses an I region which is identical to that of strain 13. However, chemical characterization of Ia.3,5 molecules isolated from these two strains has indicated that these serologically indistinguishable Ia molecules are actually chemically distinct. Ia.3,5 molecules biosynthetically labeled with either [3H]leucine, [3H]arginine, or [3H]lysine were purified by ricin affinity chromatography and isolated by indirect immunoprecipitation with specific alloantisera. Initial examination of the two Ia.3,5 molecules by SDS-PAGE, isoelectric focusing, and two-dimensional gel analyses revealed no strain-specific differences. Furthermore, comparative peptide mapping of the DHCBA and strain 13 radiolabeled Ia.3,5 alpha-chains demonstrated complete peptide homology. In contrast, tryptic peptide maps of amino acid radiolabeled beta-chains revealed two peptides unique to the strain 13 beta-chain and one peptide unique to the DHCBA beta-chain. Analysis of [3H] mannose-labeled beta-chain tryptic peptides verified that the peptide differences observed using 3H-amino acids were not due to variation in N-linked glycosylation. However, strain-specific variability was also noted in the profiles of [3H]mannose-labeled beta-chains. These data indicate that the strain 13 and DHCBA alpha-chains are probably structurally identical, while the beta-chains show strain specific alterations in their chemical structure.