Abstract
A stabilized dimeric IgA is the predominant immunoglobulin of most human exocrine secretions. During its passage through glandular cells the dimer becomes conjugated with an epithelial glycoprotein called “secretory component” (SC). IgM is also selectively transmitted through glandular epithelium (1). It has recently been proposed that SC may act as a specific epithelial Ig receptor and hence determine the selective external transfer of dimeric IgA and 19S IgM (2,3). Mach (4) first demonstrated that when dimeric IgA is mixed with free SC a spontaneous complexing occurs. He also mentioned that IgM is able to bind SC. This was independently observed by Rádl et al. (5), who claimed that only the higher polymers (25–30S) exhibit affinity for SC.
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