Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb.

摘要: Carbohydrate binding properties of a new plant lectin (GNA) isolated from snowdrop bulbs were studied using the technique quantitative precipitation, hapten inhibition, and affinity chromatography on immobilized lectin. Purified GNA precipitated highly branched yeast mannans but did not react with most glucans. Hapten inhibition experiments showed that D-mannose is an inhibitor GNA-mannan interaction neither N-acetyl-D-mannosamine nor D-glucose inhibitor. various sugars requires presence equatorial hydroxyl groups at C-3 C-4 positions axial group C-2 position D-pyranose ring. A nonreducing terminal residue necessary for oligosaccharides, oligosaccharides Man(alpha-1-3)Man units highest inhibitory potency (10-30 times greater than D-mannose) among manno-oligosaccharides tested. The hydrophobic p-nitrophenyl aglycone increased only slightly. Immobilized bound mannan bind glycogen. behavior glycoproteins high mannose type glycan chains depended density structure their chains. Glycopeptides which carry Man(alpha 1-3)Man retarded column whereas those lacking this unit or hybrid column.