SummaryThe separation of gJycoproteins as gJycoforms with specific degrees of gJycosyJation has been a problem until now. A technique involving boronate affinity chromatography has been developed to separate a heterogeneous sample of neoglycoprotein, chymotrypsin modified with maltose via reductive amination, into individual fractions with different degrees of glycosylation. Low-molecular-mass polyhydroxyl compounds, such as tris(hydroxymethyl)aminomethane (Tris), pentaerythritol, and triethanolamine proved efficient eluents clue to their ability to form strong tridentate complexes with the boronate ligand. Compounds leading to either: too strong interaction with the boronate hgand (e. g. D-sorbitol and polyvinly alcohol), or too weak or no interaction (e.g. dextran) were not suitable eluents. The study provided the opportunity to probe further into the effect of glycosylation on the function of glycoproteins.

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