Abstract
The carbohydrate composition of a human IgM myeloma protein has been studied and a particularly unusual glycopeptide purified and partially characterized. It contains 10 mannose residues and 2 N-acetylglucosamine residues in its oligosaccharide unit, N-glycosidically linked to the peptide structure of the heavy chain. Such a high quantity of mannose is not often found in the carbohydrate chains of animal glycoproteins and suggests an unusual process during the immunoglobulin glucidic chain biosynthesis.
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