Nicholson A, Austen K F
J Immunol. 1977 Jan;118(1):103-8.
Guinea pig properdin was purified to homogeneity by employing as an assay during isolation its capacity to augment the hemolytic activity of a heterologous human C3b-dependent C3 convertase, C3B. The purified protein elicited a monospecific antibody response in a rabbit. The antiserum, by immunodiffusion, gave a reaction of identity between a protein in whole guinea pig serum and the immunogen. A solid phase immunoadsorbent prepared with the antiserum removed properdin function from the purified protein. The purified guinea pig protein exhibited the classical properdin function of reconstituting a human RP for zymosan-induced C3 inactivation. The guinea pig properdin also agglutinated red cell intermediates bearing either guinea pig or human C3b and retarded the decay of homologous C3 convertase, C3B. These activities are the same as those observed for purified human properdin and validate the amplification function of properdin on terminal component activation in a second species.
通过在分离过程中利用豚鼠备解素增强异源人C3b依赖性C3转化酶C3B溶血活性的能力，将豚鼠备解素纯化至同质。纯化后的蛋白质在兔体内引发了单特异性抗体反应。通过免疫扩散，抗血清显示全豚鼠血清中的一种蛋白质与免疫原之间呈现同一性反应。用抗血清制备的固相免疫吸附剂去除了纯化蛋白质中的备解素功能。纯化后的豚鼠蛋白质表现出经典的备解素功能，即重组人RP以实现酵母聚糖诱导的C3失活。豚鼠备解素还能凝集带有豚鼠或人C3b的红细胞中间体，并延缓同源C3转化酶C3B的衰变。这些活性与纯化的人备解素所观察到的活性相同，证实了备解素在第二种物种中对末端补体成分激活的放大功能。
