Characterization and mitogenicity of a lectin from Erythrina velutina seeds
1994
Stojanovic, D. | Fernández, M. | Casale, I. | Trujillo, D. | Castes, M.
A purified lectin from Erythrina velutina was found to be a dimeric glycoprotein of Mr ca 62000 with a neutral sugar content of 5.8%. It agglutinated human A, B and O erythrocytes and rabbit red cells at minimal concentrations of 1.95 and 2.30 micrograms ml-1, respectively. In contrast, horse or cow erythrocytes were agglutinated only after neuraminidase or trypsin treatment. The haemagglutinating activity of the lectin was inhibited by D-galactose and related saccharides. N-Acetyllactosamine, the most potent inhibitor, was 95 times more effective than either lactose or galactose. N-Acetylgalactosamine was about four times as active as lactose. Asialomucin from porcine stomach, a glycoprotein rich in N-acetyllactosamine-containing O-glycans, also acted as an inhibitor. Mitogenic activity on normal human lymphocytes was obtained at an optimal concentration of ca 125 micrograms ml-1. Mononuclear cells from patients with Localized American Cutaneous Leishmaniasis proliferated in the presence of the lectin; the stimulation index was similar to that obtained with cells from healthy individuals.
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