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KMID : 0370020010150000011
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Chung-Ang Journal of Pharmacal Sciences
2001 Volume.15 No. 0 p.11 ~ p.22
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Carbohydrate-binding specificity of lectin from Maackia amurensis bark
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Abstract
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Van Damme et al. reported that Maackia amurensis bark lectin is a complex mixture of isoforms composed of two types of subunits of 32- and 37-kDa lectins, with a combined molecular weight of approximately 125 kDa. However, the binding specificity of this lectin to carbohydrates or glycoproteins is not clear. The present study confirmed that the hemagglutination activity of this lectin with human erythrocytes was inhibited by pure N-acetylneuraminic acid, and was also inhibited by fetuin, bovine submaxillary mucin, or thyroglobulin, which all contain an N-acetylneuraminic acid of oligosaccharide residues. The peroxidase-labeled Maackia amurensis lectin can detect these glycoproteins when they are present at a concentration of 0.01 mg/ml.
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