Kay M M
Acta Biol Med Ger. 1981;40(4-5):385-91.
Mechanisms by which macrophages recognize and remove senescent red blood cells (RBC) were investigated. Present evidence indicates that the antigen binding portion of immunoglobulin G (IgG) autoantibodies in normal serum selectively binds to senescent RBC in situ and initiates their removal by mononuclear phagocytes. IgG autoantibodies eluted from senescent RBC were conjugated to cyanogen bromide activated Sepharose 4B, and used to isolate and purify the IgG binding receptor. Sialoglycoprotein mixtures were processed with the senescent cell IgG affinity column. Gel electrophoresis of the bound material eluted from the column revealed a single band migrating with a molecular weight of approximately equal to 62000. This isolated peptide, but not the sialoglycoprotein mixture from which it was isolated, absorbed the phagocytosis inducing ability of IgG. Thus, the senescent cell antigen to which IgG binds, is a 62000 Dalton glycopeptide.
对巨噬细胞识别并清除衰老红细胞（RBC）的机制进行了研究。目前的证据表明，正常血清中免疫球蛋白G（IgG）自身抗体的抗原结合部分在原位选择性地结合衰老的红细胞，并启动单核吞噬细胞对其的清除。从衰老红细胞中洗脱的IgG自身抗体与溴化氰活化的琼脂糖4B偶联，并用于分离和纯化IgG结合受体。用衰老细胞IgG亲和柱处理唾液糖蛋白混合物。从柱上洗脱的结合物质的凝胶电泳显示出一条迁移的单带，其分子量约等于62000。这种分离的肽，而不是从中分离出它的唾液糖蛋白混合物，吸收了IgG的吞噬诱导能力。因此，IgG结合的衰老细胞抗原是一种62000道尔顿的糖肽。
