Blood-group-substance activity of bovine submaxillary mucin I. J activity of bovine submaxillary mucin and properties of bovine submaxillary mucin glycopeptides

• Published in: Biochimica et biophysica acta. Specialized section on mucoproteins and mucopolysaccharides Vol. 83; no. 2; pp. 209 - 217
• Main Authors: Horowitz, Martin I., Hashimoto, Yohichi, Pigman, Ward
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 07.07.1964
• Subjects: sialic acid; SA
• ISSN: 0926-6526; 1878-2280
• DOI: 10.1016/0926-6526(64)90037-0

1. 1. The presence of blood-group-substance activity in bovine saliva prompted investigation of the immunologic behavior of bovine submaxillary mucin and of glycopeptides obtained by proteolytic digestion of the mucin. 2. 2. Purified preparations of bovine submaxillary mucin inhibited hemolysis in the bovine J-anti-J system. Removal of sialic acid from the mucin by mild acid hydrolysis increased the potency of the preparation. Periodate oxidation of sialic acid free-bovine submaxillary mucin destroyed the blood-group J activity. 3. 3. Bovine submaxillary mucin exhibited a high degree of specificity. it did not inhibit other bovine blood group systems, and it was inactive in human B, M, N and I, i systems; bovine submaxillary mucin had moderate inhibition in the A and O (H) systems. 4. 4. Bovine submaxillary mucin was digested by pronase and papain (EC 3.4.4.10), and the glycopeptides were fractionated through Sephadex G-50. Glycopeptide fractions which contained the greatest amounts of hexosamine, galactose, and fucose relative to sialic acid were the best glycopeptide inhibitors of J hemolysis. 5. 5. Bovine submaxillary mucin cross-reacted with antiserum to Type XIV pneumococcal polysaccharide only after removal of sialic acid from the mucin. Possibly some d-galactosyl residues were exposed by the removal of sialic acid from bovine submaxillary mucin.