Abstract
The glycan-binding profile of a beta-galactoside-binding 15 kDa lectin (Galectin-1) purified from the oocytes of the American bullfrog, Rana catesbeiana, was studied using 61 pyridyl-aminated oligosaccharides by frontal affinity chromatography. Human blood type-A-hexasaccharide (GalNAcalpha1-3(Fucalpha1-2)Galbeta;1-4GlcNAcbeta1-4Galbeta1-4Glc) was found to exhibit the strongest ligand binding to the galectin while Forssman antigen (GalNAcalpha1-3GalNAcbeta1-3Galalpha1-4Galbeta1-4Glc) and type-A-tetrasaccharide (GalNAcalpha1-3(Fucalpha1-2)Galbeta1-4GlcNAcbeta1-4Glc) were also extensively recognized. The kinetics of affinity of galectin-1 to type-A oligosaccharide was analysed by surface plasmon resonance using neoglycoprotein with type-A oligosaccharides. R. catesbeiana oocyte galectin adhered to human rhabdomyosarcoma cells dose dependently and the activity was specifically cancelled by the neoglycoprotein. It was concluded that galectin-1 from R. catesbeiana oocytes possesses different and rare glycan-binding properties from typical members in galectin family.
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