Romans D G, Tilley C A, Crookston M C, Falk R E, Dorrington K J
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2531-5. doi: 10.1073/pnas.74.6.2531.
Reduction of interchain disulfide bonds converted some IgG incomplete antibodies to direct hemagglutinins. This conversion occurred whether antibody was free in solution or bound to the red-cell surface. Reduced antibody permitted to reoxidize in air no longer behaved as a direct agglutinin; reversion to an incomplete antibody did not occur when reoxidation was prevented by S-alkylation. These results suggest that mild reduction of the antibody imparts sufficient freedom to permit bridging between cells and are interpreted as evidence that the interheavy-chain disulfide bonds restrict segmental flexibility within the Fc fragment of IgG.
链间二硫键的还原将一些IgG不完全抗体转化为直接血凝素。无论抗体是游离于溶液中还是结合于红细胞表面，这种转化都会发生。在空气中重新氧化的还原抗体不再表现为直接凝集素；当通过S-烷基化防止重新氧化时，不会发生向不完全抗体的逆转。这些结果表明，抗体的轻度还原赋予了足够的自由度以允许细胞间的桥连，并被解释为链间二硫键限制了IgG的Fc片段内节段灵活性的证据。
