A New Marker for Neuraminidase-Treated Human Serum Glycoproteins from the Haemolymph of Tridacna maxima (Röding)

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Abstract
Highly purified human serum glycoproteins were treated with neuraminidase. The exposed subterminal carbohydrate structures reacted strongly with an anti-galactan precipitin from the hemolymph of Tridacna maxima which detects terminal, non-reducing .beta.-D-galactoside residues. This invertebrate precipitin, Tridacnin, may be used as a marker for nearly 2/3 of all asialo serum glycoproteins. A number of different cross-reactions with various other polysaccharides and galactans subdivides those neuraminidase-treated glycoproteins into several subgroups, indicating that the uncovered carbohydrate structures are not always completely identical. In this way, together with the cross-reacting precipitins from plant and invertebrate origin, Tridacnin may be a useful tool for elucidating and establishing the structure of the carbohydrate part of serum glycoproteins.