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The Effect of Non‐Immune IgG on Antigen‐Antibody Complexation
Author(s) -
ANDERSSON K.,
HANSSON U.B.,
ALKNER U.
Publication year - 1992
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.1365-3083.1992.tb02978.x
Subject(s) - immune system , antigen , chemistry , antibody , isotype , human serum albumin , immunoglobulin g , antigen antibody complex , size exclusion chromatography , albumin , immunology , biochemistry , microbiology and biotechnology , biology , monoclonal antibody , enzyme
Two preparations of human IgG, one acylated withβ‐propiolactone (acylated IgG) and one treated at pH 4 with (races of pepsin (pH 4‐IgG), were used to study the effect of non‐immune IgG on antigen antibody interactions in the antigen excess zone. Employing two immunological methods together with size‐exclusion chromatography, we found that the formation of human albumin‐rabbit anti‐human albumin complexes was inhibited in the presence of human IgG. In addition, IgG seemed to promote the aggregation of already formed complexes. Thus, non‐immune IgG may modulate immune complexation by direct molecular interactions. The effect was dependent on the size and composition of the immune complexes as well as on the conformation of the IgG molecules with respect to their shape, isotype, charge, and other surface properties. Some possible mechanisms for the reactions are discussed.