Evidence for Synthesis of Human Colostral γA as 11S Dimer

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Abstract
It is generally accepted that the secretory γA molecule in both rabbit and man is constituted by a serum type γA dimer plus an additional protein now termed secretory component (SC). It was first proposed by Tomasi et al. (1) that the secretory γA molecule was formed in plasma cells adjacent to the mucous surface and that combination with the secretory component, synthesized by glandular epithelial cells, occurred somewhere in transit of the γA molecule to the luminal surface. Examination of human colostral secretory γA isoagglutinin with anti-blood group A activity by Costea et al. (2) suggested to these investigators that the majority of the colostral secretory γA population was made up of molecules containing both κ and λ light chains. Thus, secretory γA appeared to be a hybrid molecule, implying random rather than specific combination of γA molecules.

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