Summary
In order to establish relationships between glycan structure and biological activity, the authors undertook a comparative study of the glycan primary structure of different transférons from several species. By associating permethylation-mass spectrometry and 1H-NMR spectroscopy, the primary structure of the human, bovine, caprine, murine and porcine lactotransferrin glycans were determined. Using the same methods, the glycan structure of 9 serotransferrins was determined. The results obtained led to the conclusion that glycans are specific for each transferrin and, for a given transferrin, specific to the species. No relationship could be established between primary structure and function of transferrin glycans. Glycan molecular modelling, molecular dynamics simulations and X-ray diffraction studies of free glycans confirm the mobility in space of antennae. In contrast, the glycan associated with a protein is immobilized into only one conformation, as in the case of glycan-lectin associations or of “internal” glycan-protein interactions, like in rabbit serotransferrin, in which the glycan forms a bridge between the two lobes of the peptide chain, and maintains the protein in a biologically active conformation. In the case of human sero- and lactotransferrins, the glycans are in an external position on the molecules and could play a role of recognition signals.
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Spik, G., Coddeville, B., Mazurier, J., Bourne, Y., Cambillaut, C., Montreuil, J. (1994). Primary and Three-Dimensional Structure of Lactotransferrin (Lactoferrin) Glycans. In: Hutchens, T.W., Rumball, S.V., Lönnerdal, B. (eds) Lactoferrin. Advances in, Experimental Medicine and Biology, vol 357. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2548-6_3
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DOI: https://doi.org/10.1007/978-1-4615-2548-6_3
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