A new marker for neuraminidase-treated human serum glycoproteins from the haemolymph of Tridacna maxima (Röding).
Highly purified human serum glycoproteins were treated with neuraminidase. The exposed subterminal carbohydrate structures reacted strongly with an anti-galactan precipitin from the haemolymph of Tridacna maxima which detects terminal, non-reducing beta-D-galactoside residues. This invertebrate precipitin, Tridacnin, may be used as a marker for nearly two thirds 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.
D000818:Animals; D049872:Bivalvia; D004587:Electrophoresis, Agar Gel; D005697:Galactosides / Q000032:analysis; D006023:Glycoproteins / Q000097:blood*; D006458:Hemolymph / Q000032:analysis*; D006801:Humans; D005779:Immunodiffusion; D007202:Indicators and Reagents; D009439:Neuraminidase; D011234:Precipitins
D005697:Galactosides; D006023:Glycoproteins; D007202:Indicators and Reagents; D011234:Precipitins; D009439:Neuraminidase