Structural comparisons of serologically indistinguishable H-2K-encoded antigens from inbred and wild mice.

H-2K glycoproteins from 2 wild-derived strains, B10.KPB128 and B10.GAA37, and from standard congenic lines B10.S(9R) and B10.A were compared by ion-exchange chromatography of tryptic peptides. The H-2K products of B10.S(9R) and B10.A were found to differ in about 33% of their peptides. The H-2K molecule of B10.S(9R) was indistinguishable from the H-2K molecules of B10.GAA37 and B10.KPB128. These results indicate that the H-2K-encoded products of the B10.S(9R), B10.KPB128, and B10.GAA37 lines are structurally very similar or, perhaps, identical, suggesting that some alleles of the H-2K locus may be maintained in a stable form in allopatric populations of wild mice.