Murphy B F, Saunders J R, O'Bryan M K, Kirszbaum L, Walker I D, d'Apice A J
Department of Medicine, University of Melbourne, Australia.
Int Immunol. 1989;1(5):551-4. doi: 10.1093/intimm/1.5.551.
This study examines the function of SP-40,40, a newly identified component of the SC5b-9 complement complex, in the regulation of the terminal complement pathway. Purified SP-40,40 was shown to inhibit, in a dose-dependent manner, C5b-6-initiated haemolysis. Apparently additive inhibition was also demonstrated in conjunction with complement S-protein, although SP-40,40 appears to be the more potent inhibitor on an equimolar basis. The data suggest that SP-40,40, like S-protein, probably combines with the nascent C5b-7 complex, forming a cytolytically inactive SC5b-7 - SP-40,40 complex. Preparations of S-protein, purified by an established technique, were shown to be contaminated with SP-40,40. Preparations of affinity-purified SP-40,40 were also shown to contain S-protein, suggesting that these proteins may be partially complexed in plasma.
本研究检测了SC5b-9补体复合物新鉴定成分SP-40,40在终末补体途径调控中的功能。纯化的SP-40,40呈剂量依赖性抑制C5b-6起始的溶血。与补体S蛋白联合时也表现出明显的相加抑制作用,尽管在等摩尔基础上SP-40,40似乎是更有效的抑制剂。数据表明,SP-40,40与S蛋白一样,可能与新生的C5b-7复合物结合,形成无细胞溶解活性的SC5b-7 - SP-40,40复合物。采用既定技术纯化的S蛋白制剂被证明被SP-40,40污染。亲和纯化的SP-40,40制剂也被证明含有S蛋白,这表明这些蛋白在血浆中可能部分复合。