Natural-abundance, 13C-n.m.r. spectroscopy was used to study the binding of Gd3 + to glycophorin, and also to the tetrasaccharides isolated from glycophorin after treatment of the glycoprotein with NaOH-NaBH,. Gd3+ binds to the tetrasaccharide (both in the isolated, reduced form and when still attac
13C-n.m.r.-spectral study of the mode of binding of Gd3+ to various glycopeptides
✍ Scribed by Kilian Dill; Marsha E. Daman; Ron L. Batstone-Cunningham; Jean M. Lacombe; André A. Pavia
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 580 KB
- Volume
- 123
- Category
- Article
- ISSN
- 0008-6215
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
13C-N.m.r. spectra of chondroitin 4- and 6-sulphates, chondroitin, beta-D-glucuronate, and beta-D-glucose 6-sulphate were measured in the presence of ytterbium(III) in deuterium oxide. The structure of the ytterbium-polysaccharide compounds in solution was found to be similar to that reported for ca
Four n.m.r. methods that are especially useful for characterization of oligosaccharides are applied to the trisaccharide a-NeuSAc-(2+3)-P-Gal-(l-4)-Glc (1). Three of these are two-dimensional, heteronuclear methods that provide chemical-shift correlation maps having much higher sensitivity than was
As a prelude to studies using bovine N-acetylglucosaminide-beta-(1 leads to 4)-galactosyltransferase to label membrane-surface glycoproteins with isotopically enriched D-galactose, the structural specificity of the enzymic reaction with water-soluble, hen ovalbumin has been examined. The enzyme-cata