Conversion of incomplete antibodies to direct agglutinins by mild reduction: evidence for segmental flexibility within the Fc fragment of immunoglobulin G.
Conversion of incomplete antibodies to direct agglutinins by mild reduction: evidence for segmental flexibility within the Fc fragment of immunoglobulin G.
复制标题
通过温和还原将不完整抗体转化为直接凝集素：免疫球蛋白 G Fc 片段内片段灵活性的证据。
DOI：
10.1073/pnas.74.6.2531
复制
发表时间：
1977
影响因子：
11.1
通讯作者：
K. J. Dorrington
中科院分区：
文献类型：
--
作者：
D. Romans;C. Tilley;M. Crookston;R. Falk;K. J. Dorrington
链间二硫键的还原将部分不完全抗体转化为直接血凝素。无论抗体是游离在溶液中还是结合在红细胞表面，这种转化都会发生。被允许在空气中再氧化的还原抗体不再表现为直接凝集素；当S烷基化阻止再氧化时，不会恢复为不完全抗体。这些结果表明，抗体的轻微减少给予了足够的自由以允许细胞之间的桥接，并被解释为证据，即重链间二硫键限制了Ig G Fc片段的节段灵活性。
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.