Isolation and Characterization of the Glycopeptides from a Human Immunoglobulin M

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Abstract
Five glycopeptides, designated CHO1 through CHO5, have been isolated from the heavy chain of a Waldenström IgM. Their approximate location in the molecule, their amino acid sequence and carbohydrate composition have been determined. Cleavage of the heavy chain with cyanogen bromide (CNBr) produced eight fragments, four of which were found to contain carbohydrate. CHO1 was found in CNBr-3, located toward the COOH-terminus of Fab (trypsin 60°). CHO2 was isolated from CNBr-4 located at the NH2-terminal end of Fc (trypsin 60°). CHO3 and CHO4 were found in CNBr-5 which is located in the Fc (trypsin 60°) portion of the molecule. CHO5 was isolated from CNBr-7 which is near the COOH-terminus of the heavy chain. The carbohydrate composition of CHO1 was one fucose, three mannose, one galactose and two glucosamine residues. CHO2 consisted of one fucose, six to seven mannose, two galactose and three glucosamine residues. CHO3 contained two mannose, one galactose and two glucosamine residues. CHO4 and CHO5 were of simpler composition than the other three oligosaccharides, each containing three to four residues of mannose and one to two residues of glucosamine.

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