Agaricus bisporus Lectin (ABA/ABL) - Pure

Product Description
Agaricus bisporus agglutinin/lectin (ABA/ABL) is isolated from white button mushrooms. ABA has a molecular weight of 58.5 kDa, as determined by gel filtration that corresponds to a tetramer, and has an isoelectric point that ranges between pH 5 and 6. ABA is a mixture of two phytohemagglutinins (PHA) with similar specificities for carbohydrate receptors (PHA-A and PHA-B). Each monomer has 2 distinct carbohydrate binding sites, one for galactose-Beta-1,3-N-acetylgalactosamine and another for galactose-Beta-1,3-N-acetylglucosamine. ABA elutes fetuin and Beta-D-Galactose with elution concentration of 0.2M fetuin. This lectin can bind galactose-Beta-1,3-N-acetylglucosamine but does not bind monosaccharides.

ABA has a non-specific blood group since PHA-A and PHA-B agglutinate erythrocytes independent of their blood group type. Trypsin treatment of erythrocytes decreases binding on the lectin 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 Beta-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.

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 purify specific glycoproteins, and for the purification of cells with specific surface glycoproteins.

ABA comes in lyophilized powder form and is stored below -20 C.

Applications:
IHC
Glycobiology

References

• Presant, C. and Kornfeld, S. Characterization of the cell surface receptor for the Agaricus bisporus hemagglutinin. J Biol Chem. (1972) 247(21):6937-45.
• Rueben, L., et al., Activities of lectins and their immobilized derivatives in detergent solutions. Implications on the use of lectin affinity chromatography for the purification of membrane glycoproteins. Biochemistry. (1977) 16:1787-1794
• Sueyoshi, S., et al. Purification and characterization of four isolectins of mushroom (Agaricus bisporus). Biol Chem Hoppe Seyler. Biochemistry. (1995) 366(3):213-21.