Bluestone J A, McKenzie I F, Melvold R W, Ozato K, Sandrin M S, Sharrow S O, Sachs D H
J Immunogenet. 1984 Jun-Aug;11(3-4):197-207.
Nine H-2Kb and H-2Db mutants were examined for serological differences from the wild type C57BL/6 using a panel of monoclonal antibodies (mAbs). Several differences (between the Kb mutants) were established with these mAbs. The bm3 and bm11 mutants could be distinguished serologically even though they have very similar amino acid changes. Conversely, the bm 1 and bm 10 mice, which differ in their sites of Kb mutation, express a common serological mutation, suggesting that tertiary conformation is involved in antibody binding. Both bm13 and bm14 (H-2Db mutants) exhibited profound serological alterations in H-2Db molecules when tested with mAbs that bind determinants mapping to both the NC1 and C2M domains of the Db molecule. In addition, bm13 showed altered binding of two anti-H-2Kb monoclonals.
使用一组单克隆抗体（mAb）检测了九个H-2Kb和H-2Db突变体与野生型C57BL/6之间的血清学差异。用这些mAb确定了（Kb突变体之间的）几个差异。bm3和bm11突变体尽管氨基酸变化非常相似，但在血清学上仍可区分。相反，Kb突变位点不同的bm1和bm10小鼠表现出共同的血清学突变，这表明三级构象参与了抗体结合。当用结合定位于Db分子NC1和C2M结构域的决定簇的mAb进行检测时，bm13和bm14（H-2Db突变体）在H-2Db分子中均表现出深刻的血清学改变。此外，bm13显示两种抗H-2Kb单克隆抗体的结合发生了改变。
