Petrosian M N, Vengerova T I, Rokhlin O V
Mol Biol (Mosk). 1980 Sep-Oct;14(5):1187-92.
The antigenic activity of variable (V) and constant (C) domains of mouse myeloma MOPC 21 light (L) chain has been used as a probe of their conformational state. The conformational properties of L-monomers, L-dimers and native IgG1 MOPC 21 protein were investigated by the reaction of inhibition of radioimmunoadsorbtion. Antibodies against the C-domain and different regions of V-domain were used in these experiments. It was shown that V-domain of L-monomers has sharp local conformational disruptions as compared with the native protein, while the conformational state of C-domain remains stable in monomers, dimers and native protein. It was found that the coinformational flexibility of different parts of V-domain of L-monomers is not equal. The antigenic activity of V-domain is partly restored in L-dimers, reaching the conformational state close to that of v-domain in the native protein. The possible interrelation between the conformational properties of V-domains and their functional activity is discussed.
小鼠骨髓瘤MOPC 21轻链可变（V）区和恒定（C）区的抗原活性已被用作其构象状态的探针。通过放射免疫吸附抑制反应研究了L单体、L二聚体和天然IgG1 MOPC 21蛋白的构象性质。在这些实验中使用了针对C区和V区不同区域的抗体。结果表明，与天然蛋白相比，L单体的V区有明显的局部构象破坏，而C区的构象状态在单体、二聚体和天然蛋白中保持稳定。发现L单体V区不同部分的共构象灵活性不相等。L二聚体中V区的抗原活性部分恢复，达到接近天然蛋白中v区的构象状态。讨论了V区构象性质与其功能活性之间可能的相互关系。
