Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study.

@article{Brewer1986SpecificityOC,
  title={Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study.},
  author={C. F. Brewer and L. Bhattacharyya},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 16},
  pages={
          7306-10
        }
}
We have investigated the binding of a series of high affinity asparagine-linked glycopeptides, including high mannose type and a bisected hybrid type, and several related synthetic oligosaccharides, to Ca2+- Mn2+-concanavalin A (ConA), using solvent proton nuclear relaxation dispersion (NMRD) measurements. We find that binding of the glycopeptides induces a common smaller decrease in the NMRD profile of ConA compared to that induced by monosaccharide binding. This effect is also observed with a… Expand
Formation of homogeneous cross-linked lattices between oligomannose type glycopeptides and concanavalin A.
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