Abstract
The polymerization pattern of the IgA produced by a given plasma cell tumor line is characteristic and constant. Polymerization obviously occurs through intermolecular di-sulfide interchange between labile SS bonds, but how this is regulated is not clear. Hypothetical sulfhydryl-blocking agents such as cysteine (disulfide-bonded to the crucial cysteinyls of stable monomers) have not clearly been shown to play a role. The J-chain, which is also made by IgA-producing cells, probably contributes by stabilizing the polymers but does not seem required for their formation, since IgM may polymerize without its help. In the IgA dimer the J-chain is held by disulfide bonds and occupies a hidden position (Fig. 1), as shown by antigenic analysis (1). Its incorporation occurs concomitantly with polymerization (2). All this could be the work of a disulfide-rearranging enzyme, whose activity might be the factor regulating polymerization.
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© 1974 Plenum Press, New York
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Heremans, J.F. (1974). The IgA System in Connection with Local and Systemic Immunity. In: Mestecky, J., Lawton, A.R. (eds) The Immunoglobulin a System. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4550-3_1
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DOI: https://doi.org/10.1007/978-1-4613-4550-3_1
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