Lemke H, Håmmerling G J
J Immunol. 1982 Jun;128(6):2465-9.
The spatial relationship of individual antigenic determinants on H-2Kk and H-2Db molecules was investigated with seven different monoclonal anti-H-2Kk and seven anti-H-2Db antibodies. In these studies the binding of radiolabeled monoclonal anti-H-2 to target cells was competed by addition of various cold anti-H-2 antibodies. The results indicate that on both H-2Kk and H-2Db molecules the antigenic determinants are arranged in two spatially separated clusters. Thus, antibodies to determinants within a cluster show mutual inhibition of binding but do not block the binding of antibodies to the other cluster, and vice versa. Furthermore, in the case of H-2Db antigens it was observed that binding of antibodies to one cluster would considerably enhance the binding of antibodies to the other cluster. A preliminary Scatchard analysis indicated that the enhancing antibody did not alter the affinity of the radiolabeled antibody, but led to an increase of available binding sites on the cell membrane. In addition, binding inhibition studies revealed that the conventional private specificity H-2.2 of H-2Db consists of at least two independent sites on the molecule.
利用七种不同的抗H-2Kk单克隆抗体和七种抗H-2Db抗体，研究了H-2Kk和H-2Db分子上各个抗原决定簇的空间关系。在这些研究中，通过加入各种冷抗H-2抗体来竞争放射性标记的抗H-2单克隆抗体与靶细胞的结合。结果表明，在H-2Kk和H-2Db分子上，抗原决定簇都排列成两个空间上分离的簇。因此，针对一个簇内决定簇的抗体显示出结合的相互抑制，但不会阻断抗体与另一个簇的结合，反之亦然。此外，在H-2Db抗原的情况下，观察到抗体与一个簇的结合会显著增强抗体与另一个簇的结合。初步的Scatchard分析表明，增强抗体不会改变放射性标记抗体的亲和力，但会导致细胞膜上可用结合位点的增加。此外，结合抑制研究表明，H-2Db的传统私有特异性H-2.2由分子上至少两个独立的位点组成。
