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J. Biol. Chem., Vol. 264, Issue 1, 173-177, 01, 1989
N Kochibe and KL Matta
A lectin in the fruiting bodies of Psathyrella velutina was purified by
affinity chromatography on a chitin column and subsequent ion-exchange
chromatography. P. velutina lectin (PVL) tends to aggregate irreversibly in
buffered saline, but the addition of glycerol (10%, v/v) to lectin
solutions was found to prevent aggregate formation. PVL is assumed to occur
as a monomer of a polypeptide of Mr = 40,000 as determined by gel
filtration and by gel electrophoresis in the presence of sodium dodecyl
sulfate. PVL is specific for N-acetylglucosamine (GlcNAc). It was
determined by equilibrium dialysis to have four binding sites/polypeptide
molecule showing an average intrinsic association constant of K0 = 6.4 x
10(3) M-1 toward this sugar. The binding specificity of the lectin was
studied by hemagglutination inhibition assays and by avidin-biotin-mediated
enzyme immunoassays using various GlcNAc-containing saccharides. The
results indicate that methyl N-acetyl beta-glucosaminide was a slightly
better inhibitor than the corresponding alpha-anomer. PVL binds well to
oligosaccharides bearing nonreducing terminal beta-GlcNAc linked 1----6 or
1----3 but poorly to those having a 1----4 linkage, such as N-acetylated
chito- oligosaccharides. It also binds to the subterminal GlcNAc moiety
when it is substituted at the C-6 position but does not interact with the
moiety when substituted either at C-3 or C-4. Thus, these results show that
PVL is quite different in its binding specificity from other GlcNAc-binding
lectins of higher plants since they bind preferentially to beta-GlcNAc in
1----4 linkage and they have a high affinity for chitin oligosaccharides.
Purification and properties of an N-acetylglucosamine-specific lectin from Psathyrella velutina mushroom
Department of Biology, Faculty of Education, Gunma University, Maebashi, Japan.
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