Canine secretory immunoglobulin M, isolated from both colostrum and bronchial secretions, contained the unique glycoprotein bound secretory component. The presence of this extra subunit accounted for the differences in size, quaternary structure, and antigenicity observed upon comparison of secretory immunoglobulin M with its serum counterpart. Approximately 90% of the isolated secretory immunoglobulin M contained covalently bound secretory component while, in the remainder of the population, secretory component was loosely attached and easily dissociated from the immunoglobulin. Following peptide bond cleavage with cyanogen bromide, the release of bound secretory component and J chain from secretory immunoglobulin M was not detected. Because cyanogen bromide cleavage of secretory immunoglobulin A results in the release of these subunits, differences in the primary structure of secretory immunoglobulin M and secretory immunoglobulin A must exist around the binding sites for secretory component and J chain.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of Immunology|
|State||Published - 1977|
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