Abstract
A number of oligomannosides and glycopeptides prepared from various sources were tested for their potency to inhibit the binding of 3H-mannotetraitol (Manalpha1 leads to Manalpha1 leads to Manalpha1 leads to 2Mannitol) to antimannan antibodies. It was found that antimannan antibodies are highly specific to the Manalpha1 leads to 3Man structure, reacting very poorly with the Manalpha1 leads to 2Man and Manalpha1 leads to 6Man structures. A Manalpha1 leads to 3Man structure at the non-reducing end is far more reactive than one at an inner position. In this respect, antimannan antibodies differ from concanavalin A which reacts with mannose residues substituted at C-2 as well as those at non-reducing ends. Glycopeptides prepared from ovalbumin, Taka amylase A and from membrane glycoproteins of rat liver cross-reacted with antimannan antibodies to various extents reflecting the characteristic structures of the individual glycopeptides.
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