Abstract
Bovine submaxillary mucin, after removal of its sialic acid component, is cleaved by trypsin into two principal glycopeptide fractions; their final yield corresponds to 70% by weight of the original mucin and 85% of the original amount of hexosamine in the mucin. These glycopeptides have amino acid and carbohydrate compositions that are very similar to those of the original and desialyzed mucin. The main glycopeptide contains about 28 amino acids; the second one seems to be a covalently linked trimer of the former and is resistant to further action by trypsin. The protein core of bovine submaxillary mucin is composed mainly of several hundred covalently bound sequences of these glycopeptides. These results are compatible with those reported by Downs and Pigman (1969) for the products obtained by chemical cleavage of this mucin.
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