Lämmler C, Guszczynski T, Dobryszycka W
Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität, Giessen.
Zentralbl Bakteriol Mikrobiol Hyg A. 1988 Nov;269(4):454-9. doi: 10.1016/s0176-6724(88)80067-1.
Certain group A streptococci with surface antigen T 4 possess surface receptors for human haptoglobin (Hp). Binding of 125I Hp 2-1 to two representative group A streptococcal cultures could be inhibited by unlabelled Hp 2-1, Hp 2-2 and Hp 1-1 but not by the alpha 1, alpha 2 or beta chains of Hp. Hp complexes formed with equine hemoglobin and asialo-Hp also reduced 125I-Hp 2-1 binding to group A streptococci. Hp binding proteins could be solubilized from streptococcal surface by hot acid treatment of the bacteria and purified by subsequent affinity chromatography on human Hp 2-1 sepharose. The isolated Hp binding proteins specifically inhibited 125I-Hp 2-1 binding to group A streptococci and retained their 125I-Hp 2-1 binding activity in a dot binding assay on nitrocellulose membranes. SDS-PAGE and protein blots of Hp binding proteins developed with 125I-labeled Hp 2-1 revealed numerous high molecular weight proteins with 125I-Hp 2-1 binding activity.
某些带有表面抗原T4的A组链球菌具有人触珠蛋白（Hp）的表面受体。未标记的Hp 2-1、Hp 2-2和Hp 1-1可抑制125I Hp 2-1与两种代表性A组链球菌培养物的结合，但Hp的α1、α2或β链则无此作用。与马血红蛋白和去唾液酸Hp形成的Hp复合物也可减少125I-Hp 2-1与A组链球菌的结合。通过对细菌进行热酸处理可从链球菌表面溶解Hp结合蛋白，随后通过在人Hp 2-1琼脂糖凝胶上进行亲和层析进行纯化。分离出的Hp结合蛋白可特异性抑制125I-Hp 2-1与A组链球菌的结合，并在硝酸纤维素膜的斑点结合试验中保留其125I-Hp 2-1结合活性。用125I标记的Hp 2-1进行SDS-PAGE和蛋白质印迹分析显示，有许多具有125I-Hp 2-1结合活性的高分子量蛋白质。
