Wheat germ agglutinin (WGA) contains a group of closely related isolectins, with an
isoelectric point about pH 9. The receptor sugar for WGA
is N-acetylglucosamine,
with preferential binding to dimers
and trimers of this sugar. WGA can bind oligosaccharides
containing terminal N-acetylglucosamine or chitobiose,
structures which are common to many serum and membrane
glycoproteins. Bacterial cell wall peptidoglycans, chitin,
cartilage glycosaminoglycans, and glycolipids can also bind
WGA. Native WGA has also been reported to interact with
some glycoproteins via sialic acid residues (see succinylated
WGA). This lectin is used for the purification of insulin
receptors and for neuronal tracing.
Inhibiting/Eluting Sugar: Chitin Hydrolysate or 500 mM
N-acetylglucosamine with salt and/or acid elution generally required
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