Properties of α-galactosidase II(2) from Vicia faba seeds.

Abstract:

:α-Galactosidase II(2) (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. 3·10(3) 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 II(2) have been discussed in relation to both V. faba lectin (favin) and other legume α-galactosidases.

journal_name

Planta

journal_title

Planta

authors

Dey PM,Naik S,Pridham JB

doi

10.1007/BF00446377

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

114-8

issue

1

eissn

0032-0935

issn

1432-2048

journal_volume

167

pub_type

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