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Two Lectins, designated FVL-1 and FVL-2, were isolated and purified from the fruiting bodies of edible mushroom Flammulina veluripes using ammonium sulfate fractionation, ethanol treatment, DEAE-TOYPEARL ion-exchange column chromatography, and TSK-Gel HW-55F column chromatography. Specific activity increased 18 folds for FVL-1 and 7.9 folds for FVL-2 from ethanol treated sample. SDS-PAGE of FVL-1 and FVL-2 gave apparent molecular mass of 10.6 kDa and 37 kDa, respectively. FVL-2 agglutinated all type of human erythrocytes (A, B, AB, and O). However, FVL-1 agglutinated more human erythrocyte type O than type A, B, and AB. The hemagglutination activities of the FVL-1 were effectively inhibited by bovine submaxillary and porcine stomach mucins(BSM and PSM), fetuin, asialofetuin and cations, such as Cu^(2+), Mg^(2+), Ca^(2+), Mn^(2+) and Fe^(2+). However, FVL-2 was not inhibited by any cations. The hemagglutination activities of the two lectins were not inhibited by the sugar, such as lactose, galactose and sugar derivatives. FVL-1 and FVL-2 were stable at pH 5∼11 and pH 4∼7, respectively. FVL-1 was stable below 55℃ and FVL-2 was below 45℃.
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