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Highly purified human mucins from postmortem intestinal tissue were fractionated on anion exchange columns to generate separate neutral and acidic species. The neutral mucin (less than 1.0 mol % sialic acid) was the major species (greater than 80% by weight) and contained a higher molar proportion of fucose, galactose, and N-acetylglucosamine, and a lower proportion of sialic acid and N-acetylgalactosamine than the acidic species (greater than 10 mol % sialic acid). Amino acid analyses revealed a highly significant enrichment in serine, aspartate, and alanine in the neutral species and proline, threonine, and glycine in the acidic species. Thiol reduction of each species to remove their integral 118,000-dalton component did not alter the essential interspecies differences. Differences in threonine, proline, and serine also remained after removal of all "naked" or pronase-susceptible peptide regions from each species. These results indicate that neutral and acidic mucins contain glycopeptide segments exclusive of their 118,000-dalton and naked peptide components, which differ in amino acid composition. The key amino acid markers are similar to those observed for fuco- and sialoglycopeptides obtained after proteolytic digestion of human colonic mucin by Gold et al. (Gold, D.V., Schochat, D., and Miller, F. (1981) J. Biol. Chem. 256, 6354-6358). The oligosaccharide composition of small intestinal and colonic mucin may therefore depend upon transcriptional control of the synthesis of specific mucin peptides as well as the post-translational activity of glycosyltransferases. These findings may have significance for the quality and functions of mucus produced in a variety of pathological states.
Wesley et al. (Mon,) studied this question.