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The Reaction of Rheumatoid Anti‐Gm Antibodies with Native and Aggregated Gm‐Negative IgG
Author(s) -
GAARDER P. I.,
NATVIG J. B
Publication year - 1974
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.1365-3083.1974.tb01289.x
Subject(s) - autoanalyzer , antibody , chemistry , isotype , immunology , antigen , hemagglutination , rheumatoid arthritis , hemagglutination assay , microbiology and biotechnology , population , biology , medicine , titer , chromatography , monoclonal antibody , environmental health
Rheumatoid anti‐Gm(a) antibodies were shown to react with native Gm(a‐) IgG. This reaction takes place with the C H 3 domain (pFc' fragment) of IgG and is not due to anti‐isotype specificities contaminating the test system. The reactivity of the Gm(a‐) IgG is greatly increased by heat aggregation, and this increase is clearly related to the amount of aggregates formed. Rheumatoid anti‐Gm(a) reacts with aggregated IgG1. IgG2. and IgG3 Gm(g+) proteins but not with IgG3 Gm(b+) or IgG4 proteins. Thus there is a clear specificity in the reactions with aggregated IgG of different subclasses. Quantitative hemagglutination inhibition studies in the AutoAnalyzer suggested that the antigenic determinants of native and aggregated Gm(a+) or Gm(a‐) IgG involved in the reaction with rheumatoid anti‐Gm(a) were very similar. Furthermore, immunosorbent studies showed that the saint population of rheumatoid anti‐Gm(a) antibodies is reacting with the native and aggregated Gm(a+) and Gm(a‐) IgG Analogous findings were obtained using rheumatoid anti‐Gm(b 1 ) and anti‐Gm(g).