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Activation of complement by endotoxin.

Ovine erythrocytes (E) coated with endotoxin (LPS) from Salmonella typhosa 0901 have been used for characterization of the nature of a pathway by which LPS activates complement (C). E-LPS consumed C in normal guinea-pig serum in a manner identical to that in which C is consumed by LPS, that is, with marked consumption of C3-C9 and little depletion of C1, C4, and C2. A "natural" y2-globulin, isolated from serum by ion-exchange chromatography, was required for C-mediated lysis of E-LPS in dilute serum. When it was reacted with guinea-pig y2-globulin, C1, C4, and C2, followed by C-EDTA, E-LPS was lysed. Deletion of y2-globulin, C1, C4, or C2 from the reaction prevented lysis. The small amounts of the early-acting components of C used indicated that it would be difficult to measure their loss in whole serum after incubation with LPS. This