Sugar binding specificities of anti-H(O) lectins disclosed by use of fucose-containing human milk oligosaccharides as binding inhibitors.
The binding to normal and sialidase-treated human erythrocytes of six 125I-labeled lectins [Ulex europeus lectin I (UEA-1) and II (UEA-II), Laburnum alpinum lectins I (LAA-I) and II (LAA-II), and Cytisus multiflorus lectins I (CMA-I) and II (CMA-II)], was studied in detail. Quantitative inhibition assays of the lectin binding to the cells were also performed with various human milk oligosaccharides as inhibitors. Based on a comparison of the inhibition constants of the inhibitors thus obtained with the association constants of the lectins to the cells, the relative activities of cell surface blood group antigens toward the lectins are discussed.
Konami
Y
Y
Tsuji
T
T
Toyoshima
S
S
Matsumoto
I
I
Osawa
T
T
D050260:Carbohydrate Metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D005260:Female; D005643:Fucose / Q000032:analysis / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism*; D009439:Neuraminidase / Q000494:pharmacology; D009844:Oligosaccharides / Q000032:analysis / Q000494:pharmacology*
D037102:Lectins; D009844:Oligosaccharides; D005643:Fucose; D009439:Neuraminidase