Further definition of the size of the blood group-i antigenic determinant using a chemically synthesised octasaccharide of poly-N-acetyllactosamine type
1992; Elsevier BV; Volume: 228; Issue: 1 Linguagem: Inglês
10.1016/s0008-6215(00)90566-4
ISSN1873-426X
AutoresTen Feizi, Elizabeth F. Hounsell, Jocelyne Alais, Alain Veyrières, Serge David,
Tópico(s)Monoclonal and Polyclonal Antibodies Research
ResumoIn earlier studies, the minimum structure which inhibited the binding of anti-i to an i-active glycoprotein was the linear trisaccharide, β-d-Galp-(1 → 4)-β-d-GlcpNAc-(1 → 3)-d-Gal. There was an increasing hierarchy of inhibitory activities in the linear tetrasaccharide, β-d-Galp-(1 → 4)-β-d-GlcpNAc-(1 → 3)-β-d-Galp-(1 → 4)-β-d-GlcNAc, its methyl β-glycoside, and in the methyl β-glycoside of the hexasaccharide. The linear octasaccharide methyl β-glycoside in this series is approximately only half as active as the hexasaccharide methyl β-glycoside. Analyses by high resolution 1H-n.m.r. of these two oligosaccharides indicated that they have similar conformations in solution, and there is no evidence for the occurrence of inter-molecular interactions which might partially hinder the binding of anti-i to the octasaccharide methyl β-glycoside. These results are consistent with the size of the i antigen being in the region of a hexasaccharide. It is proposed that the methyl aglycon group of the hexasaccharide methyl β-glycoside confers an above normal activity by presenting a hydrophobic area for additional contact in the vicinity of the antibody-combining site.
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