Abstract
Erythrina variegata lectin was purified by affinity chromatography with lactose-Sepharose 6B. The purified lectin was homogenous on poly crylamide gel electrophoresis, immunoelectrophoresis, and Sephadex G-150 gel filtration. The molecular weight of the lectin was 60, 000 by the gel filtration, and SDS-polyacrylamide gel electrophoresis gave a single band at a position corresponding to the molecular weight of 29, 000, indicating that the lectin is a dimer composed of two identical subunits. The lectin was a glycoprotein with its neutral sugar content being 9%. It contained high amounts of acidic and hydroxy amino acids, a low amount of methionine, and no cysteine. This lectin agglutinated human erythrocytes of O type at a concentration of 4 μg/ml, which was inhibited most potently by p-nitrophenyl-β-D-galactopyranoside among the sugars tested, suggesting the importance of the hydrophobic contribution of the aromatic region in the sugar binding-activity. Galactose and its related sugars were also inhibitory but to lesser extents.
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