Müller F, Segerling M
Immunology. 1974 Jul;27(1):33-41.
By consecutive euglobulin precipitation, gel filtration (Sephadex G-200/G-100), di-ethylaminoethyl (DEAE) and carboxy-methyl (CM 52) cellulose column chromatography a protein that has an enhancing effect on immune immobilization of was isolated from guinea-pig serum (Immobilization Accelerating Factor (IAF). The final isolation product was shown to be in a state of functional purity. IAF does not contain any of the known haemolytic complement subunits (C1—C9) or the muramidase lysozyme involved in immune immobilization of . The sedimentation rate of IAF was estimated to be 8.1S. The approximate molecular weight was shown to be 150,000. The purified factor increased the number of immobilized treponemes in the modified immobilization test by more than 50 per cent.
通过连续优球蛋白沉淀、凝胶过滤（葡聚糖G - 200/G - 100）、二乙氨基乙基（DEAE）和羧甲基（CM 52）纤维素柱色谱法，从豚鼠血清中分离出一种对[具体物质]免疫固定有增强作用的蛋白质（免疫固定加速因子（IAF））。最终分离产物显示处于功能纯态。IAF不包含任何已知的溶血补体亚基（C1 - C9）或参与[具体物质]免疫固定的溶菌酶。IAF的沉降率估计为8.1S。其近似分子量显示为150,000。在改良的[具体物质]免疫固定试验中，纯化因子使固定的梅毒螺旋体数量增加了50%以上。
