Inoue K
Department of Bacteriology, Osaka University Medical School, Japan.
Complement Inflamm. 1989;6(3):219-22. doi: 10.1159/000463095.
After activation of serum complement, a neoantigen was reported to appear on a 54,000-dalton fragment of C5. On the other hand, a monoclonal antibody (MoAb), No. 568, revealed that an epitope on the beta-chain of C5 became masked after the formation of SC5b-9 complex. Murine MoAbs were obtained to human C5a-des-Arg. Some of them are specific only to C5a-des-Arg but not to C5a or C5. Using these MoAbs, a sandwich immunoassay was devised for detection and measurement of C5a-des-Arg. The neoepitopes for these MoAbs were analyzed by their reactivities to synthetic peptide derivatives of human and porcine C5a, and the structural changes of C5a were suggested to occur after the removal of the carboxyl terminal arginine residue.
血清补体激活后,据报道在C5的一个54,000道尔顿片段上出现了一种新抗原。另一方面,一种单克隆抗体(MoAb),编号568,显示在SC5b-9复合物形成后,C5β链上的一个表位被掩盖。获得了针对人C5a-去精氨酸的鼠单克隆抗体。其中一些仅对C5a-去精氨酸具有特异性,而对C5a或C5无特异性。利用这些单克隆抗体,设计了一种夹心免疫测定法用于检测和测量C5a-去精氨酸。通过这些单克隆抗体与人和猪C5a的合成肽衍生物的反应性分析了它们的新表位,并提示C5a在去除羧基末端精氨酸残基后会发生结构变化。