Glycopeptides of immunoglobulins. Investigations on IgA myeloma globulins.
The oligosaccharide units of a type K and a type L IgA immunoglobulin have been examined. The two proteins differed in their content of 6-deoxy-l-galactose and N-acetylneuraminic acid, and in the d-mannose/d-galactose ratio. With glycopeptides prepared from the type K protein, specific glycosidases liberated the N-acetylneuraminic acid and 7-8 residues of 2-acetamido-2-deoxy-d-glucose, and mild acid hydrolysis released most of the 6-deoxy-l-galactose. The type K immunoglobulin appeared to contain 3 oligosaccharide units, whereas the type L protein probably contained 3 or more units.
D000596:Amino Acids / Q000032:analysis; D002854:Chromatography, Paper; D006023:Glycoproteins / Q000032:analysis*; D006026:Glycoside Hydrolases; D006801:Humans; D008970:Molecular Weight; D009101:Multiple Myeloma; D005719:gamma-Globulins / Q000032:analysis*
D000596:Amino Acids; D006023:Glycoproteins; D005719:gamma-Globulins; D006026:Glycoside Hydrolases