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- W1999996816 abstract "Abstract The nature of the glucose/mannose specific lectin activity of α-galactosidase I from Vicia faba seeds has been examined. Gel filtration in the presence of high concentrations of glucose and SDS-PAGE failed to detect favin, a classical lectin which also occurs in the seed. A comparison of the haemagglutinating activities of the α-galactosidases from Vigna radiata and V. faba seeds strongly suggests that the catalytic site of the Vigna enzyme is also responsible for its agglutinating activity and that the catalytic and lectin sites are at different loci in the case of V. faba α-galactosidase I. The latter conclusion is supported by an investigation of the effects of glucose, mannose and galactose on the catalytic and lectin activities and by results obtained by demetallization of the V. faba enzyme. A single galactose-binding site and two mannose binding sites per subunit of enzyme I were detected by the method of equilibrium dialysis and the association constants for these monosaccharides measured. Mannose did not appear to affect the binding of galactose to the enzyme or vice versa . The removal of glycan chains from α-galactosidase I with endo-β- N -acetylglucosaminidase H released an active dimeric form of α-galactosidase. The possible involvement of lectin-glycoprotein interactions in the stabilization of the tetrameric form of the enzyme is considered." @default.
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- W1999996816 date "1986-04-01" @default.
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- W1999996816 title "Further characterization of α-galactosidase I-glycoprotein lectin from Vicia faba seeds" @default.
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- W1999996816 doi "https://doi.org/10.1016/s0031-9422(00)81549-6" @default.
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