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Related Experiment Videos

Mechanism of IgM polymerization.

R M Chapuis, M E Koshland

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1974
    PubMed
    Summary

    The J chain acts as a disulfide clasp, linking two subunits within pentameric IgM. This finding clarifies the initial steps in IgM assembly, starting with J-containing dimers.

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    Area of Science:

    • Immunology
    • Structural Biology
    • Biochemistry

    Background:

    • Pentameric IgM is a crucial antibody in the innate immune system.
    • The role of the J chain in IgM structure and assembly has been previously investigated.
    • Understanding IgM's quaternary structure is key to its function.

    Purpose of the Study:

    • To determine the precise stoichiometry of the J chain in pentameric IgM.
    • To elucidate the disulfide linkage of the J chain within the IgM structure.
    • To propose a model for IgM assembly based on J chain interactions.

    Main Methods:

    • Radiolabeling of thiols in IgM constituent chains.
    • Complete reduction and alkylation of pentameric IgM.
    • Limited reduction and alkylation to analyze subunit dissociation and J chain disulfide cleavage.

    Main Results:

    • One mole of J chain is disulfide-bonded to one mole of pentameric IgM.
    • J chain disulfide bonds did not directly correlate with the extent of IgM depolymerization.
    • No J chain disulfides were cleaved in J-containing dimer products from limited reduction, indicating J chain's internal role.

    Conclusions:

    • The J chain functions as a disulfide clasp, bridging two IgM monomer subunits.
    • This structural role suggests IgM assembly initiates with the formation of J-chain-containing dimers.
    • A model of sequential disulfide exchanges is proposed for IgM polymerization.

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