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Modulation of the Assembly of Immunoglobulin Subunits by J Chain

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The Immunoglobulin a System

Abstract

Because J chain is present in polymeric and not monomeric immunoglobulin molecules and since it is released from polymers when they are reduced to subunits, it has been suggested that J chain plays an important role in the assembly of both IgA and IgM polymers. J chain has been reported (1) to have a high half cystine content (10–12 per mole), and there are, therefore, sufficient cysteine residues to undergo disulfide bond formation with each of the subunits in a pentameric immunoglobulin molecule. Consistent with this thesis are quantitative estimates of the amount of J chain in IgM and IgA suggesting that there is one J chain per mole of polymer regardless of the polymeric size.

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References

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Author information

Authors and Affiliations

  1. Department of Immunology, Mayo Medical School Mayo Foundation, 55901, Rochester, Minnesota, USA

    Thomas B. Tomasi Jr. & S. Hauptman

Authors
  1. Thomas B. Tomasi Jr.
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  2. S. Hauptman
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Editor information

Editors and Affiliations

  1. Institute of Dental Research Departments of Microbiology and Medicine, University of Alabama in Birmingham, Birmingham, Alabama, USA

    Jiri Mestecky

  2. Departments of Pediatrics and Microbiology, University of Alabama in Birmingham, Birmingham, Alabama, USA

    Alexander R. Lawton

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© 1974 Plenum Press, New York

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Tomasi, T.B., Hauptman, S. (1974). Modulation of the Assembly of Immunoglobulin Subunits by J Chain. In: Mestecky, J., Lawton, A.R. (eds) The Immunoglobulin a System. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4550-3_12

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  • DOI: https://doi.org/10.1007/978-1-4613-4550-3_12

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4552-7

  • Online ISBN: 978-1-4613-4550-3

  • eBook Packages: Springer Book Archive

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