, Volume 167, Issue 1, pp 114–118 | Cite as

Properties of α-galactosidase II2 from Vicia faba seeds

  • P. M. Dey
  • S. Naik
  • J. B. Pridham


α-Galactosidase II2 (MW ∼ 43 390) from resting Vicia faba L. seeds had been shown to possess d-glucose/d-mannose-specific lectin activity. Inhibition studies with monosaccharides and an examination of the effects of heat and pH on the catalytic and lectin activities of the enzyme indicate that the enzyme substrate and the lectin haptens bind at different sites on the protein. d-Mannosebinding has been investigated by equilibrium dialysis and spectrophotometrically. Both methods yield Ka values of approx. 3·103 M-1 for the interaction and there would appear to be two mannosebinding sites per molecule of enzyme protein. The lectin properties of V. faba α-galactosidase II2 have been discussed in relation to both V. faba lectin (favin) and other legume α-galactosidases.

Key words

Favin α-Galactosidase Lectin Vicia (α-galactosidase) 


con A

concanavalin A


carboxymethyl cellulose


molecular weight


p-nitrophenyl α-d-galactoside


sodium dodecyl sulphate


polyacrylamide-gel electrophoresis


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Copyright information

© Springer-Verlag 1986

Authors and Affiliations

  • P. M. Dey
    • 1
  • S. Naik
    • 1
  • J. B. Pridham
    • 1
  1. 1.Department of BiochemistryRoyal Holloway CollegeEghamUK

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