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Introduction A new type of pharmaceuticals became available when the recombinant DNA technique was introduced. The development of cell systems for manufacturing of biologically important proteins, used in therapy and diagnosis, have focused the attention on protein glycosylation. Most of the events leading to N-glycosylation involving transfer of the lipid-linked oligosaccharide to asparagine in a certain amino acid sequence of the nascent protein and subsequent processing to the final products have been elucidated. The glycosylation pattern obtained depends on several factors such as cell types and growth conditions. An N-glycosylation site carries either a complex or a high mannose type of structure. Hybrid structures are sometimes found but in rather rare cases. Structural diversity is often prevalent resulting in presence of different structures (bi-, tri-, and tetraantrennary) in the same glycosylation site. Furthermore, heterogeneity within the structures is common, due to partial substitution by sialic acid and fucose. This structural heterogeneity makes the isolation and the following structural analysis difficult. 0-Glycosylation means substitution of serine or threonine usually with N-acetylgalactosamine in an 0-glycosidic linkage. Unlike the N-glycosylation no specific amino acid sequence is required for 0-glycosylation. The 0-linked carbohydrate chains are often smaller and structurally less complicated than the N-linked. The present poper summarizes methods for release, separation and structural analysis of Nand 0linked glycoprotein oligosaccharides. は じめに

Structural Determination of the Glycan Part in Glycoproteins.