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Naturally Occurring Polymers of IgA Lacking J Chain
Author(s) -
TOMASI T. B.,
CZERWINSKI D. S.
Publication year - 1976
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.1365-3083.1976.tb03014.x
Subject(s) - depolymerization , j chain , chemistry , in vitro , albumin , alpha chain , polymer , immunoglobulin a , biochemistry , immunoglobulin light chain , myeloma protein , secretory component , polymer chemistry , biology , antibody , immunology , immunoglobulin g , gene , organic chemistry
Two of twenty IgA myeloma proteins studied were found to lack J chain. Both IgA proteins contained dimers and higher polymers (trimers, tetramers, pentamers) in proportions similar to those found in most classical ‘J‐positive’ proteins. Both the ‘J‐negative’ proteins contained bound albumin and alpha‐1 anti‐trypsin (α1AT), and reduction with mercaptoethylamine caused a release of albumin and α1AT concomitant with depolymerization of the higher polymers of IgA. These proteins formed complexes with secretory component (SC) in vitro, indicating that the presence of J chain is not a requirement for SC binding.