Summary
A full-length cDNA coding for human lactoferrin was isolated from a mammary gland library and the recombinant protein was expressed in BHK cells as described by Stowell et al. (1991). Two N-linked glycans from purified recombinant lactoferrin were released by hydrazinolysis and analyzed by 400-MHz 1H-NMR spectroscopy. The identified structures corresponded to N-acetyllactosaminic biantennary glycans and were α-2,3-disialylated forms (80%) or α-2,3-monosialylated (20%) forms. Moreover, 70% of total glycans were α-1,6-fucosylated at the GlcNAc residue linked to asparagine. In regard to its glycan moiety, the recombinant glycoprotein is close to native lactoferrins from milk or leukocytes, but shows specific structural features that should be taken into account prior to in vivo and in vitro biological studies.
See p. 116 for list of abbreviations to be used in this chapter.
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Legrand, D., Salmon, V., Coddeville, B., Benaïssa, M., Plancke, Y., Spik, G. (1997). Structural Determination of Two N-Linked Glycans Isolated from Recombinant Human Lactoferrin Expressed in BHK Cells. In: Hutchens, T.W., Lönnerdal, B. (eds) Lactoferrin. Experimental Biology and Medicine, vol 28. Humana Press. https://doi.org/10.1007/978-1-4612-3956-7_7
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