期刊
PROTEIN AND PEPTIDE LETTERS
卷 16, 期 6, 页码 677-684出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986609788490104
关键词
American bullfrog (Rana catesbeiana); blood type-A hexasaccharide; cell adhesion activity; frontal affinity chromatography; galectin-1
资金
- JSPS (Japan Society for the Promotion of Science) [0760110001]
- Yokohama City University [K20002]
- Ministry of Education, Culture, Science, Sports, and Technology (MEXT), Japan
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 (GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GlcNAc beta 1-4Gal beta 1-4Glc) was found to exhibit the strongest ligand binding to the galectin while Forssman antigen (GalNAc alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc) and type-A-tetrasaccharide (GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GlcNAc beta 1-4Glc) 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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