Webster G F, McArthur W P
Int Arch Allergy Appl Immunol. 1981;66(3):304-9. doi: 10.1159/000232834.
The ability of pyran copolymer to interact with the classical and alternative pathways of complement was assessed in human and C4-deficient guinea pig serum. Pyran induced a dose-dependent inhibition of hemolytic activity in both serum systems. Immuno-electrophoretic analysis of pyran-treated human serum revealed that C3 was not cleaved. Factor B was altered into a more anionic mobility which was not similar to biologically cleaved Ba or Bb fragments. Pyran-treated serum was unable to lyse antibody-coated erythrocytes (EA or EA coated with C1 and C4 and EA coated with C1, C4 and C2. Pretreatment of serum with ethylenediaminetetraacetic acid did not prevent inhibition of hemolytic activity by pyran. Cobra venom factor did not cleave C3 in the presence of pyran. These data indicate that pyran does not activate complement by standard mechanisms but does inhibit one or more of its components.
在人血清和C4缺陷豚鼠血清中评估了吡喃共聚物与补体经典途径和替代途径相互作用的能力。吡喃在两种血清系统中均诱导了溶血活性的剂量依赖性抑制。对经吡喃处理的人血清进行免疫电泳分析显示，C3未被裂解。B因子转变为具有更高阴离子迁移率的形式，这与经生物学裂解产生的Ba或Bb片段不同。经吡喃处理的血清无法裂解抗体包被的红细胞（EA或包被有C1和C4的EA以及包被有C1、C4和C2的EA）。用乙二胺四乙酸预处理血清并不能阻止吡喃对溶血活性的抑制。在有吡喃存在的情况下，眼镜蛇毒因子不能裂解C3。这些数据表明，吡喃不是通过标准机制激活补体，而是抑制其一种或多种成分。
