S蛋白独立于补体激活以及珠子上末端补体复合物的形成，与经血清处理的琼脂糖珠结合。
S protein binds to serum-treated agarose beads independently of complement activation and the formation of the terminal complement complex on the beads.
作者信息
Hetland G, Garred P, Pettersen H B, Mollnes T E, Johnson E
机构信息
Blood Bank, Ullevaal Hospital, Oslo, Norway.
出版信息
Clin Exp Immunol. 1990 Mar;79(3):459-62. doi: 10.1111/j.1365-2249.1990.tb08112.x.
Comparison of initial (early-phase) and terminal (late-phase) sequence activation of complement by agarose beads and endotoxin was evaluated in an enzyme immunoassay (EIA) of serum levels of C3c and C9 neoepitopes, respectively. EIA and Western blotting with anti-S protein monoclonal antibody revealed lower S protein values and weaker S protein bands in serum activated by agarose beads than by endotoxin, implying that S protein was removed from serum by binding to agarose. The binding of S protein to the beads was confirmed by radioimmunoassay and was found to be equal in normal and heat-inactivated serum. In contrast, the terminal complement complex was formed only on agarose beads incubated with normal serum and not with inactivated serum.
分别通过酶免疫测定法（EIA）检测血清中C3c和C9新表位水平，评估琼脂糖珠和内毒素对补体初始（早期阶段）和终末（晚期阶段）序列激活的情况。酶免疫测定法和使用抗S蛋白单克隆抗体的蛋白质印迹法显示，与内毒素激活的血清相比，琼脂糖珠激活的血清中S蛋白值较低，S蛋白条带较弱，这意味着S蛋白通过与琼脂糖结合而从血清中去除。通过放射免疫测定法证实了S蛋白与珠子的结合，并且发现在正常血清和热灭活血清中这种结合是相同的。相反，终末补体复合物仅在与正常血清孵育的琼脂糖珠上形成，而不在与灭活血清孵育的琼脂糖珠上形成。
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