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Solubilization of immune precipitates by complement in the absence of properdin or factor D
Author(s) -
Späth P.J.,
Pascual M.,
Meyer-Hänni Liselotte,
Schaad U.B.,
Schifferli J.A.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81318-8
Subject(s) - properdin , solubilization , chemistry , complement system , alternative complement pathway , bovine serum albumin , antibody , antiserum , complement factor b , classical complement pathway , immune system , precipitation , complement (music) , size exclusion chromatography , complement control protein , biochemistry , immunology , biology , enzyme , physics , meteorology , complementation , gene , phenotype
Various experiments have demonstrated that immune precipitates (IPs) are not solubilized by complement in the absence of alternative pathway function. To determine whether the characteristics of the IPs were responsible for these observations, we studied the solubilization (Sol) of IPs formed by bovine serum albumin (BSA)‐rabbit antiBSA and tetanus toxoid (TT)‐human antiTT. Sera deficient in properdin solubilized a fraction of BSA‐antiBSA precipitates, although only when the IPs were formed in antibody excess. The same sera solubilized TT‐antiTT precipitates with some delay but almost as efficiently as normal serum. Factor D‐depleted serum solubilized a fraction of TT‐antiTT precipitates too, indicating that Sol may proceed through activation of the classical pathway only. Thus, the requirements for complement‐mediated Sol depend on the characteristics of the IPs and do not necessarily include alternative pathway function.