Lectin from Agaricus bisporus / Mushroom, Lyophilized powder. Agaricus bisporus agglutinin (ABA) is a mixture of two phytohemagglutinins with similar specificities for carbohydrate receptors (PHA-A and PHA-B). Both PHA-A and PHA-B are heterogeneous by SDS-PAGE. The mushroom PHA will have a molecular weight of 58.5 kDa as determined by gel filtration that corresponds to tetramer. Each monomer has 2 distinct carbohydrate s, one for galactose-β-1,3-N-acetylgalactosamine and another for galactose-β-1,3-N-acetylglucosamine.
PHA-A and PHA-B agglutinate erythrocytes independent of their blood group type. Trypsin treatment of erythrocytes decreases lectin binding to the cell surface. The O-linked glycopeptide released by trypsin is a potent inhibitor of both the isolectins. Removal of the terminal sialic acid residue from the glycopeptide increases its inhibitory potency 8-fold. Periodate or β-galactosidase treatment of the trypsin released glycopeptide destroys all inhibitory activity. Simple sugars are very poor inhibitors of these isolectins. However, a galactose residue appears to play a major role in these lectin binding mechanisms. The sugar linkage is also important since a synthetic N-linked glycopeptide is not inhibitory, while the O-linked glycopeptide released by trypsinization is a potent inhibitor. The cell receptor for the isolectins has the structure Galactose-Gal-NAc-ser (or threonine).
Lectin that recognizes O-linked galactose-β-1,3-N-acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T-disaccharide), present on cell surface glycoproteins. ABA can also bind galactose-β-1,3-N-acetylglucosamine. ABA does not bind monosaccharides. ABA can be internalized by clathrin-coated vesicles after binding to surface glycoproteins. After internalization, it inhibits nuclear import of nuclear localization signal dependent proteins. ABA inhibits proliferation of malignant cells without cytotoxicity for normal cells. ABA can be used to recognize and purifiy specific glycoproteins, and for the purification of cells with specific surface glycoproteins. ABA has potential as anti-proliferative agent.
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