Grey H M, Mannik M
J Exp Med. 1965 Sep 1;122(3):619-32. doi: 10.1084/jem.122.3.619.
Dissociated H and L chains of human gammaG-myeloma proteins were recombined by removal of conditions interrupting non-covalent interactions. In the process of recombination 7S molecules were formed. It was demonstrated that the H chains from individual gammaG-myeloma proteins recombine with their own L chains but also with L chains derived from other myeloma proteins. In some instances, however, the L chains from other myeloma proteins did not recombine as avidly with the H chains as the autologous L chains. The specificity of the non-covalent interactions of H and L chains was particularly well brought out by competitive recombination experiments where an individual H chain had a choice of recombining with its own L chain or with the L chain obtained from another myeloma protein. In this manner a spectrum of affinities between individual H chains and several L chains was demonstrated. In the vast majority of recombinations there was a clearcut preference for recombination to take place between the H and L chains derived from the same protein. It is postulated that this specificity is related to differences in the primary structure, which cause differences in configuration of these homogeneous H and L chains and that these configurations then dictate on thermodynamic grounds the pairing of H chains with particular L chains.
通过去除打断非共价相互作用的条件，将人γG-骨髓瘤蛋白的解离重链和轻链进行重组。在重组过程中形成了7S分子。结果表明，来自单个γG-骨髓瘤蛋白的重链不仅能与其自身的轻链重组，还能与源自其他骨髓瘤蛋白的轻链重组。然而，在某些情况下，来自其他骨髓瘤蛋白的轻链与重链重组的亲和力不如自身轻链。重链和轻链非共价相互作用的特异性在竞争性重组实验中得到了特别好的体现，在该实验中，单个重链可以选择与其自身轻链或从另一种骨髓瘤蛋白获得的轻链重组。通过这种方式，证明了单个重链与几种轻链之间存在一系列亲和力。在绝大多数重组中，明显倾向于源自同一蛋白的重链和轻链之间发生重组。据推测，这种特异性与一级结构的差异有关，一级结构的差异导致这些同源重链和轻链的构象不同，然后这些构象基于热力学原理决定了重链与特定轻链的配对。
