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J. Biol. Chem., Vol. 267, Issue 2, 707-713, 01, 1992
T Endo, H Ohbayashi, K Kanazawa, N Kochibe and A Kobata
The carbohydrate binding specificity of Psathyrella velutina lectin (PVL)
was thoroughly investigated by analyzing the behavior of various
complex-type oligosaccharides and human milk oligosaccharides on a PVL-
Affi-Gel 10 column. Basically, the lectin interacts with the nonreducing
terminal beta-N-acetylglucosamine residue, but does not show any affinity
for the nonreducing terminal N-acetylgalactosamine or N-acetylneuraminic
acid residue. Substitution of the terminal N- acetylglucosamine residues of
oligosaccharides by galactose completely abolishes their affinity to the
column. GlcNAc beta 1----3Gal beta 1---- 4sorbitol binds to the column, but
GlcNAc beta 1----6Gal beta 1---- 4sorbitol is only retarded in the column.
The behavior of degalactosylated N-linked oligosaccharides is quite
interesting. Although all degalactosylated monoantennary sugar chain
isomers are retarded in the column, those with the GlcNAc beta 1----2Man
group interact more strongly with the column than those with the GlcNAc
beta 1----4Man group or the GlcNAc beta 1----6Man group. The
degalactosylated bi- and triantennary sugar chains bind to the column, but
the tetraantennary ones are only retarded in the column. These results
indicated that the binding affinity is not simply determined by the number
of terminal N-acetylglucosamine residues. Addition of the bisecting
N-acetylglucosamine residue reduces the affinity of oligosaccharides to the
column, but addition of an alpha-fucosyl residue at the C-6 position of the
proximal N-acetylglucosamine residue does not affect the behavior of
oligosaccharides in the column. These results indicated that the binding
specificity of PVL is quite different from those of other
N-acetylglucosamine-binding lectins from higher plants, which interact
preferentially with the GlcNAc beta 1---- 4 residue.
Carbohydrate binding specificity of immobilized Psathyrella velutina lectin
Department of Biochemistry, University of Tokyo, Japan.
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