Abstract
Soybean (Glycine max L.) seeds contain a galactose-binding protein which displays two activities: (a) an α-galactosidase activity and (b) a hemagglutinin activity. The α-galactosidase-hemagglutinin was purified to homogeneity by conventional protein purification procedures and also by affinity chromatography. This protein can be easily separated from soybean agglutinin, the N-acetyl-d-galactosamine-specific lectin in soybean. Further, these two agglutinins show no immunological relatedness. The α-galactosidase-hemagglutinin can be reversibly converted by pH changes from a tetrameric form which displays both enzymic and hemagglutinin activities to a monomeric form which displays enzymic activity only. Although both the monomeric and tetrameric forms are enzymically active, they display different pH optima and carbohydrate specificities.
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