N-linked neutral sugar chains of aminopeptidase N purified from rat small intestinal brush-border membrane.

摘要: Neutral oligosaccharides, which accounted for 74% of the total N-linked sugar chains released by hydrazinolysis rat small intestinal aminopeptidase N, were investigated on a structural basis. They are mainly composed complex-type with tri- and tetraantennary structures, amounts high mannose type (7% neutral chains) also included. The unique feature is most them contain terminal N-acetylglucosamine residues blood group H antigenic determinants in their outer chain moieties, bisecting trimannosyl cores. Both 1H 2H found, but former expressed at distal portions moieties oligosaccharides.