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Interference by Rheumatoid Factor and Clq in the Detection of IgG Complexes: Studies of Model Systems by ELIS A
Author(s) -
WAGER O.,
LINDSTRÖM P.
Publication year - 1982
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1982.tb00655.x
Subject(s) - chemistry , rheumatoid factor , immune system , competitive binding , interference (communication) , microbiology and biotechnology , immunology , antibody , biochemistry , medicine , biology , receptor , channel (broadcasting) , electrical engineering , engineering
Interference by purified IgM rheumaloid factors (RFs) and Clq in the detection of model complexes was studied by enzyme‐linked immunosorbent assay (ELISA). Soluble monoclonal and polycloral cryoglobulin IgM RFs und human or porcine Clq inhibited dosedepcndently the binding of human IgG complexes to solid‐phase IgM RF, Clq, and bovine conglutinin (Kg). The inhibition patterns of the Kg binding were dependent on the order of confrontation between the reactants. To achieve inhibition, Clq or RF had to he offered lo the complexes before treatment with fresh normal human serum (NHS); complexes pretreated with fresh NHS (alexinated complexes) were resistant to inhibition. Heating at 56 °C or 63 °C, which destroyed the alexinating capacity of NHS, did not affect the Kg binding of alexinated complexes. On the basis of present and previous findings it is concluded that intrinsic Clq and RFs are likely to interfere with detection of circulating immune complexes (CICs) in Clq‐ or RF‐binding assays; they are less likely to interfere with detection of CICs in Kg‐binding assays. The problems associated with selective removal of intrinsic Clq and RFs are discussed.