Structure of the carbohydrate chain of free secretory component from human milk.
Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid. Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain. In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues. The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases. Sugars released from the glycopeptide by various glycosidases were also quantitated. From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
D000596:Amino Acids / Q000032:analysis; D001216:Asparagine; D001224:Aspartic Acid / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D005260:Female; D006020:Glycopeptides / Q000302:isolation & purification; D006801:Humans; D007128:Immunoglobulin Fragments / Q000302:isolation & purification; D008745:Methylation; D008895:Milk, Human / Q000276:immunology*; D011247:Pregnancy; D011402:Pronase; D012635:Secretory Component / Q000302:isolation & purification
D000596:Amino Acids; D002241:Carbohydrates; D006020:Glycopeptides; D007128:Immunoglobulin Fragments; D012635:Secretory Component; D001224:Aspartic Acid; D001216:Asparagine; D011402:Pronase