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
Plantajournal_title
Plantaauthors
Dey PM,Naik S,Pridham JBdoi
10.1007/BF00446377subject
Has Abstractpub_date
1986-01-01 00:00:00pages
114-8issue
1eissn
0032-0935issn
1432-2048journal_volume
167pub_type
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