Secretory component, the receptor for polymeric immunoglobulin, has nothing to do with beta-galactosyltransferase in human milk.

Secretory component (SC) in external secretions is a soluble form of the polymeric immunoglobulin-receptor that is expressed on the cell membrane of mucosal epithelial cells. beta-(1-4)galactosyl transferase (beta-GT) is an enzyme that transfers galactose to non-reducing N-acetylglucosamine residues on various glycoproteins and is present in a soluble form in secretions as well as in a membrane-bound form. beta-GT is considered to have affinity for glycoproteins, including IgA in secretion. It has been claimed that these two proteins are related to or identical with each other. In the present study, we defined that the SC and the beta-GT are each independent molecules by the following facts; (1) both molecules are separable either by antibody-affinity chromatography, conventional ion-exchange or molecular exclusion chromatography, (2) conventionally purified SC from human milk contained neither enzymatic activity or antigenic determinants of the beta-GT, (3) recombinant beta-GT does not show reactivity with antibodies to SC, and (4) the SC showed no reactivity with antibody to beta-GT.