Novel Subunit in Secretory IgA

@article{Halpern1970NovelSI,
  title={Novel Subunit in Secretory IgA},
  author={M. Halpern and M. E. Koshland},
  journal={Nature},
  year={1970},
  volume={228},
  pages={1276-1278}
}
A new component, “J” (for joining), has been found in rabbit and human secretory IgA in addition to the S, α, and light chains already characterized. J has a molecular weight of approximately 23,000 and, by contrast with the S component, is disulphide-linked to the α chain. It is present in the dimer but not the monomer form of human IgA myelomas, and therefore seems to be responsible for the dimer structure characteristic of secretory IgA. 
Biosynthesis of J-chain in mouse IgA and IgM.
Association of S-IgA subunits.
Naturally Occurring Polymers of IgA Lacking J Chain
Variable J‐chain content in human IgM
Role of J Chain in Secretory Immunoglobulin Formation
Studies on human secretory immunoglobulin A. 3. J chain.
J chain in pig immunoglobulins.
  • J. Zikán
  • Chemistry, Medicine
  • Immunochemistry
  • 1973
The origin of monomeric and polymeric forms of IgA in man.
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