Green PJ, Tamatani T, Watanabe T, Miyasaka M, Hasegawa A, Kiso M, Yuen CT, Stoll MS, Feizi T High affinity binding of the leucocyte adhesion molecule L-selectin to 3'-sulphated-Lea and -Lex oligosaccharides and the predominance of sulphate in this interaction demonstrated by binding studies with a series of lipid-linked oligosaccharides Biochemical and Biophysical Research Communications188 (1992)
244-251
NCBI PubMed ID:1384480 Journal NLM ID:0372516 Publisher: Academic Press Institutions: Glycoconjugates Section, MRC Clinical Research Centre, Harrow, Middlesex, U.K
The binding of the leucocyte adhesion molecule L-selectin has been investigated toward several structurally defined lipid-linked oligosaccharides immobilized on silica gel chromatograms or plastic wells. In both assay systems the 3'-sulphated Le(a)/Le(x) type tetrasaccharides [formula: see text] were more strongly bound than 3'-sialyl analogues. A considerable binding was observed to the 3'-sulphated oligosaccharide backbone in the absence of fucose but not to a 3'-sialyl analogue or fuco-oligosaccharide analogues lacking sulphate or sialic acid. Affinity for other sulphated saccharides: 3'-sulphoglucuronyl neolactotetraosyl ceramide and glycolipids with sulphate 3'-linked to terminal or sub-terminal galactose or N-acetylgalactosamine was detected in the chromatogram assay only. These studies, together with earlier reports that L-selectin binding to endothelium is inhibited by sulphatide, highlight the relative importance of sulphate in the adhesive specificity of this protein.
Related record ID(s): 100059, 107859 NCBI Taxonomy refs (TaxIDs):36025 Reference(s) to other database(s): GTC:G62939PF, CCSD:43769, CBank-STR:13598 Show glycosyltransferases
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(later renamed to: Nakazawaea holstii; Pichia holstii)