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J. Biol. Chem., Vol. 263, Issue 2, 728-734, 01, 1988
N Shibuya, IJ Goldstein, EJ Van Damme and WJ Peumans
Carbohydrate binding properties of a new plant lectin (GNA) isolated from
snowdrop bulbs were studied using the technique of 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 of GNA-mannan interaction but neither
N-acetyl-D-mannosamine nor D-glucose is an inhibitor. Hapten inhibition
with various sugars showed that GNA requires the presence of equatorial
hydroxyl groups at the C-3 and C-4 positions and an axial group at the C-2
position of the D-pyranose ring. A nonreducing terminal D-mannose residue
is necessary for the interaction of oligosaccharides, and oligosaccharides
with terminal Man(alpha-1-3)Man units showed the highest inhibitory potency
(10-30 times greater than D-mannose) among the manno-oligosaccharides
tested. The presence of the hydrophobic p-nitrophenyl aglycone increased
the affinity of D-mannose only slightly. Immobilized GNA bound yeast mannan
but did not bind glycogen. The behavior of glycoproteins with high mannose
type glycan chains depended on the density and the structure of their
glycan chains. Glycopeptides which carry Man(alpha 1-3)Man units were
retarded on the immobilized GNA column whereas those lacking this unit or
with hybrid type glycan chains were not retarded on the column.
Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
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