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The interaction of elderberry sambucus sieboldiana bark lectin and sialyloligosaccharides as detected by proton nmr


The interaction of elderberry sambucus sieboldiana bark lectin and sialyloligosaccharides as detected by proton nmr



Journal of Biochemistry (Tokyo) 112(1): 143-146



The interaction of Japanese elderberry bark lectin (Sambucus sieboldiana agglutinin, SSA) with carbohydrate was investigated by H-NMR. When a low affinity ligand, methyl .beta.-D-galactoside (.beta.MeGal), was mixed with SSA, each proton signal of .beta.-MeGal was broadened. The signal of H-4 was markedly broad, while those of H-1, OCH3, and H-2 of .beta.MeGal were rather sharp. The specific broadening of Gal H-4 was more evident when SSA was mixed with methyl-.beta.-D-lactoside (.beta.MeLac). Position-dependent signal broadening suggests that .beta.MeGal binds to SSA such that H-4 is closely involved in the contact region, but H-1, OCH3, and H-2 are far from this region. In the case of a high affinity ligand, Neu5Ac (.alpha.2-6)Gal(.beta.1-4)Glc(=N6L), ligand signals of the SSA-N6L mixture did not change at all. But when a small amount of N6L was added to the SSA-.beta.MeGal mixture, the broad signals of bound .beta.MeGal became dramatically sharp. This indicates that the added N6L molecules liberated the bound .beta.MeGal from SSA. On the other hand, the sialyllactose with the .alpha.(2-3)-linkage(=N3L) could not substitute for bound .beta.MeGal because of its lower affinity. This demonstrates that the competitive binding experiment between two ligands is a useful technique to detect the interaction of lectins with high affinity ligands which could not be observed directly by NMR signal broadening and/or chemical shift change.

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Related references

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