Abstract
Although the three-dimensional structure of human lactoferrin, in various functional states, has been determined by X-ray crystallographic analysis at high resolution (Baker et al, this volume) there are good reasons to investigate the structures of lactoferrins of other species. The sequence variations which occur between species result in subtle changes in properties and offer the opportunity to more closely analyse the relationships between structure and function. Moreover the structural work on human lactoferrin has identified various elements of flexibility (Baker et al, 1991), which could be expressed in species variations.
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Haridas, M., Anderson, B.F., Baker, H.M., Norris, G.E., Baker, E.N. (1994). X-Ray Structural Analysis of Bovine Lactoferrin at 2.5 Å Resolution. 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_24
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DOI: https://doi.org/10.1007/978-1-4615-2548-6_24
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