Shinomiya T, Koyama J
J Biochem. 1975 Sep;78(3):435-41. doi: 10.1093/oxfordjournals.jbchem.a130926.
The intradermal catabolism of antibodies injected in guinea pigs to provoke skin reactions was studied using 125I-labeled guinea pig IgG1 and IgG2 anti-ovalbumin antibodies. Disappearance of both the IgG1 and IgG2 antibodies from injected sites was accelerated by intravenous injection of the antigen. The antigen-antibody complexes produced in vitro were also catabolized more rapidly than free antibodies, when estimated using 125I-labeled antibodies. On the other hand, the catabolism of normal IgG2 was not influenced by local anaphylactic reaction elicited by IgG1 antiovalbumin antibody coexisting at the sites. Therefore, the enhanced catabolism of antibodies on challenge was not caused by increased vascular permeability due to anaphylactic reactions, but by more rapid elimination of immune complexes formed at the sites. The Fc parts of IgG1 and IgG2 antibodies played an essential role in the enhancement of catabolism since the catabolism of the F(ab')2 fragments was not accelerated by complex formation with ovalbumin, but rather reduced.
使用125I标记的豚鼠IgG1和IgG2抗卵清蛋白抗体，研究了注射到豚鼠体内以引发皮肤反应的抗体的皮内分解代谢。静脉注射抗原可加速注射部位IgG1和IgG2抗体的消失。当使用125I标记的抗体进行评估时，体外产生的抗原-抗体复合物的分解代谢也比游离抗体更快。另一方面，正常IgG2的分解代谢不受存在于该部位的IgG1抗卵清蛋白抗体引发的局部过敏反应的影响。因此，激发时抗体分解代谢增强不是由过敏反应导致的血管通透性增加引起的，而是由该部位形成的免疫复合物更快清除所致。IgG1和IgG2抗体的Fc部分在分解代谢增强中起重要作用，因为F(ab')2片段与卵清蛋白形成复合物后，其分解代谢并未加速，反而减慢。
