Studies on lectins. XXXVIII. Isolation and characterization of the lectin from black locust bark (Robinia pseudacacia L.).
The lectin of black locust (Robinia pseudacacia) bark was isolated by specific adsorption on formaldehyde-fixed human erythrocytes and elution with a borate solution. The lectin is homogeneous on disc electrophoresis and ultracentrifugation (s20,w = 5.8 S) but yields three bands on isoelectric focusing. It has a molecular weight of approximately 110,000 and consists of two types of subunit (mol. wt 29,000 and 31,500). Its pI is approximately 5.9; it contains high amounts of aspartic acid, threonine and serine, no cysteine and very little methionine. Also 7.2% of covalently bound neutral sugar and 0.47% of glucosamine are present. The lectin is nonspecific in agglutination of human erythrocytes, it is inhibited by high concentrations of N-acetyl-D-galactosamine and is mitogenic in rabbit lymph node lymphocytes.
D000596:Amino Acids / Q000032:analysis; D004912:Erythrocytes; D006384:Hemagglutination; D006801:Humans; D037102:Lectins / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D037121:Plant Lectins; D010944:Plants / Q000032:analysis*
D000596:Amino Acids; D037102:Lectins; D046911:Macromolecular Substances; D037121:Plant Lectins