Carbohydrate specificity of lectins from Boletopsis leucomelas and Aralia cordate.
The carbohydrate specificity of three novel lectins, Boletopsis leucomelas lectin (BLL), Aralia cordate lectin (ACL), and Wasabia japonica lectin (WJL), was examined by frontal affinity chromatography using a panel of fluorescently labeled 47 oligosaccharides. The results indicate that BLL recognizes an agalacto structure of the biantennary chain and its bisecting structure. ACL showed strong affinity for triantennary oligosaccharides, but no affinity for tetraantennary structure. WJL showed no appreciable affinity for any of the 47 glycans examined. These lectins with a unique affinity specificity might be useful for examining alterations in the glycan structures of the glycoconjugates in association with development and various diseases.
Laboratory of Cellular Biochemistry, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, Japan.
Yu
Y
Koyama
Takuji
T
Suzuki
Shoji
S
Odani
Sachiko
S
Nakamura
Junko
J
Kominami
Jun
J
Hirabayashi
Mamoru
M
Isemura
D027983:Aralia / Q000737:chemistry*; D001487:Basidiomycota / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008968:Molecular Conformation; D013379:Substrate Specificity
D002241:Carbohydrates; D037102:Lectins