Colling R G, Brown J C
Infect Immun. 1981 Dec;34(3):828-34. doi: 10.1128/iai.34.3.828-834.1981.
Cold agglutinin antibodies were isolated from group C streptococcal antisera by thermal elution from rabbit erythrocytes. These antibodies reacted with bovine submaxillary mucin, fetuin, immunoglobulin G, and the Fc fragment of immunoglobulin G in hemolytic inhibition assays. Further, in radioimmunoassay these antibodies reacted with the major glycopeptide fragment of rabbit immunoglobulin G. Affinity-purified group carbohydrate-specific antibodies reacted weakly with glycopeptide. These data suggest that certain populations of antibody in group C streptococcal antisera may participate in tissue reactivity via interaction with cell surface glycoproteins, including immunoglobulin G.
通过从兔红细胞进行热洗脱,从C组链球菌抗血清中分离出冷凝集素抗体。在溶血抑制试验中,这些抗体与牛下颌粘蛋白、胎球蛋白、免疫球蛋白G以及免疫球蛋白G的Fc片段发生反应。此外,在放射免疫测定中,这些抗体与兔免疫球蛋白G的主要糖肽片段发生反应。亲和纯化的组碳水化合物特异性抗体与糖肽的反应较弱。这些数据表明,C组链球菌抗血清中的某些抗体群体可能通过与包括免疫球蛋白G在内的细胞表面糖蛋白相互作用而参与组织反应性。