In 1939, Sorensen & Sorensen discovered a red protein in bovine milk. This component, now usually called lactoferrin, is a glycoprotein with a γ-electrophoretic mobility, and consists of a single polypeptide chain with a molecular weight of 77,000. Like serum transferrin, it binds two ferric ions, but it differs in its amino acid composition, immunological properties and in the higher stability of its iron-complex at acid pH. These features apply to bovine as well as to human lactoferrin (Groves, 1960; Johansson, 1960; Montreuil, Tonnelat & Mullet, 1960; Blanc & Isliker, 1961; Masson & Heremans, 1968; Castellino, Fish & Mann, 1970; Querinjean, Masson & Heremans, 1971).
In the human, lactoferrin is not only found in milk but also occurs in other external secretions. It is synthesized by three types of tissues: the acini
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