Biochemical analyses of the H-2K-gene products of the C57BL/6 mutant strains, bm3 and bm11, have been carried out in order to characterize the structural relationships among these antigens. From comparative tryptic peptide mapping of cyanogen bromide fragments from the mutant and parent Kb glycoproteins and from preliminary amino-acid sequence analyses, a number of discrete differences have been discerned. Two sites of difference at amino residues 77 and 89 in the Kbm3 glycoprotein are noted relative to Kb. An alteration at residue 77 similar or identical to that seen in Kbm3 is present in the K antigen of the bm11 mutant. Because our techniques sample only 75 to 80 percent of the extracellular portion of H-2Kb, other undetected changes are possible. However, our present findings are most consistent with the conclusion that only very limited differences exist between mutant and parent molecules. Further, taken together with CML (cell-mediated-lymphocytotoxicity) reaction patterns (Melief et al. 1980), the biochemical data support the hypothesis that the proposed structural alterations in the Kb mutant glycoproteins are directly related to their observed immunological specificity.