Protein pattern, ammonia content, glutamine synthetase activity, lipid peroxidation, superoxide dismutase, catalase, peroxidase and peroxidase isoforms were studied in the leaves and roots of 7-d-old peanut (Arachis hypogaea L. cv. JL-24) seedlings treated by 25, 100 and 250 μM jasmonic acid (JA). SDS-PAGE protein profile of leaves and roots after JA application showed a significant increase in 18, 21, 30, 45, 47 and 97.4 kDa proteins and significant decrease in 22 and 36 kDa proteins. Pathogenesis related PR-18 was specific in leaves at 250 μM JA and PR-21 have cross reacted differently with 21 and 30 kDa proteins in leaves and roots treated by all JA concentrations. Further, the immunoblot analysis with glutamine synthetase, GS-45 antibodies revealed a specific cross reaction with 45 and 47 kDa proteins of both control and JA treated leaves, however, higher at 100 and 250 μM JA treated leaves than control ones. Further, the malondialdehyde (MDA) content significantly increased in leaves and roots treated with JA, indicated membrane damage with JA treatments that led to the generation of peroxidation products. The peroxidase isozymic pattern showed two specific isoforms. Besides, the activities of SOD and catalase were significantly elevated in JA treated leaves.

from Vicia faba seeds has been resolved into three molecular forms, I, II' and II', respectively.Enzyme I is a tetramer (Mr 160000) consisting of identical sub-units (Mr 44000 f 2000). All three forms display lectin activity with glucose/mannose specificity. Enzyme I has been further studied with respect to its lectin specificity and various factors affecting this property. The results indicate that the catalytic and the lectin sites reside in the same protein molecule. The results presented are unique in that the enzyme activity is specific for galactose and its Iectin activity is specific for glucose/mannose. Vicia faba cu-Galactosidase

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.

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