Abstract
The glycosylated amyloid light chain protein EPS was isolated from amyloid fibrils from the liver of a patient with Waldenstrom's macroglobulinemia. A tryptic glycopeptide of EPS (200 nmol) was isolated and characterized by 1H-n. m. r. The glycopeptide was digested with N-glycanase and the released oligosaccharides analyzed by high performance anion exchange chromatography. The monosaccharide composition and the linkage of the different oligosaccharides were determined by methanolysis and methylation analysis. The NMR spectrum revealed a bisected biantennary oligosaccharide as the main structure. HPAEC-PAD demonstrated the presence of several other related glycans in the glycopeptide preparation.