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Blocking Effect of J Chain and J‐Chain Antibody on the Binding of Secretory Component to Human IgA and IgM
Author(s) -
BRANDTZAEG P.
Publication year - 1975
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.1365-3083.1975.tb03725.x
Subject(s) - j chain , secretory component , blocking (statistics) , secretory iga , component (thermodynamics) , antibody , chain (unit) , heavy chain , immunoglobulin light chain , blocking antibody , chemistry , immunology , microbiology and biotechnology , biology , computer science , physics , computer network , astronomy , thermodynamics
Isolated released J chain showed only a small affinity for free secretory component (SC), as indicated by a marginal but reproducible blocking effect on the binding of SC to Ig polymers. The SC‐binding site was completely blocked by J‐chain antibody in those Ig polymers where the bound J chains were accessible to the antibody. Along with the established masking effect of SC on the antigenicity of J chains present in secretory IgA, these results are compatible with the idea that the conformation of Ig‐associated J chains contributes to the SC‐binding site of Ig polymers.