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Occurrence, structure, biochemical properties and technological characteristics of lactoferrin

Published online by Cambridge University Press:  09 March 2007

Jan M. Steijns*
Affiliation:
DMV International, R&D Center, PO Box 13, 5460 BA Veghel, The Netherlands
A. C. M. van Hooijdonk
Affiliation:
DMV International, R&D Center, PO Box 13, 5460 BA Veghel, The Netherlands
*
*Corresponding author: Dr. Jan Steijns, DMV International, Center of Expertise for Nutrition, PO Box 14, 6700 AA Wageningen, The Netherlands, fax +31 317 475 769, email: steijnsj@dmv-international.com
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Abstract

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The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine secretions, has been elucidated in great detail, both the three-dimensional protein structure and the attached N-glycans. Structure–function relationships are being established. From these studies a function for lactoferrin in host defence and modulation of iron metabolism emerges. This paper describes in some detail how iron and other cations may be bound by lactoferrins from human or bovine sources and elucidates parts of the molecule that are critical for interactions with cells and biomolecules. Furthermore, the technological aspects, more specifically the heat-sensitivity, of bovine lactoferrin in different matrices are described.

Type
Research Article
Copyright
Copyright © The Nutrition Society 2000

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