Biochemical comparison of H-2K antigen isolated from C3HfB/HeN and C3H/HeN mice

Abstract

The H-2K glycoproteins were isolated from spleen cells of C3H/HeN and C3HfB/Hen mice and compared by tryptic peptide mapping techniques. The two antigens were found to be very similar in that more than 90 percent of detectable peptides appeared identical. However, two lysine-containing peptide present in tryptic digests of H-2K antigens isolated from C3H mice were absent from tryptic digests of H-2K antigens isolated from C3Hf mice. This was probably not the result of altered glucosylation since neuramindase digestion demonstrated that the disparate peptides were not glycopeptides but most probably resulted from substitution of one or two amino acids in the H-2K molecule of C3HfB/HeN mice. These differences were small but significant and demonstrated that H-2Kk (C3H) and H-2Kkv1 (C3Hf) antigens are structurally distinct. This is compatible with the observed reciprocal skin-graft rejection, MLR, and generation of cytotoxic T lymphocytes between the two strains. The significance of this finding in conjunction with what is known about properties of 1-ethyl-1-nitrosourea-induced tumors of C3Hf mice is discussed.