| Literature DB >> 2489042 |
B F Murphy1, J R Saunders, M K O'Bryan, L Kirszbaum, I D Walker, A J d'Apice.
Abstract
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.Entities:
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Year: 1989 PMID: 2489042 DOI: 10.1093/intimm/1.5.551
Source DB: PubMed Journal: Int Immunol ISSN: 0953-8178 Impact factor: 4.823