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The Journal of Immunology, 1973, 110: 840-847.
Copyright © 1973 by The American Association of Immunologists, Inc.

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Isolation and Characterization of the Glycopeptides from a Human Immunoglobulin M1

Mary M. Hurst, William Niedermeier, Jiri Zikan2 and J. Claude Bennett

Department of Microbiology and the Division of Clinical Immunology and Rheumatology of the Department of Medicine, School of Medicine, University of Alabama in Birmingham, Birmingham, Alabama 35294

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.

Footnotes

1 These studies were supported by grants from the National Institutes of Health, Bethesda, Maryland and the John A. Hartford Foundation, Inc., New York.

2 Current address: Czechoslovak Academy of Sciences, Institute of Microbiology, Department of Immunology, Prague, Czechoslovakia.







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