Abstract
Recent studies on polymeric immunoglobulins have demonstrated the presence of a small polypeptide chain, the J chain, in addition to the heavy and light chains that comprise the monomer units (1,2). The presence of J chain in covalent disulfide linkage within these polymers and its absence from all forms of monomeric immunoglobulins strongly suggests that J plays a fundamental role in establishing and maintaining the polymeric state. In order to understand this role, several questions must be answered. First, what is the stoichiometry of J chain in the various polymeric forms? Second, is J chain linked to every heavy chain in the polymer, or merely to one or two? Third, is J an obligatory requirement for correct polymer formation, or can normal covalent polymers be assembled in the absence of J chain? When this information has been obtained, a mechanism for the assembly of immunoglobulin polymers can be developed.
Supported by USPHS Grant AI-07079-07
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© 1974 Plenum Press, New York
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Koshland, M.E., Wilde, C.E. (1974). Mechanism of Immunoglobulin Polymer Assembly. In: Mestecky, J., Lawton, A.R. (eds) The Immunoglobulin a System. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4550-3_14
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DOI: https://doi.org/10.1007/978-1-4613-4550-3_14
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