Bovine lactoferrin properties

Lactoferrin has been isolated and identified from a wide variety of animal species. However, most of the studies on structure and iron-binding properties have involved either human or bovine proteins (2). Lactoferrin closely resembles transferrin in molecular weight of 75,000 to 90,000 and consists of a single polypeptide chain that binds two ferric ions. The pi of transferrin is 5.9 while that of lactoferrin is approximately 9.0 (8) and has an even higher association constant for iron-binding. Lactoferrin has the property of retaining its iron even in the presence of a relatively low-affir-nity iron chelator such as citrate below pH 4.0. Transferrin, on the other hand, looses its iron when the pH is lowered from 6 to 5 (7). There is extensive information in the literature concerning the physical properties of lactoferrin which will not be covered in this paper. 

Researchers (Nuijens et al., 1997) at the Leiden University (the Netherlands) in collaboration with Pharming, NV (Leiden, the Netherlands) compared recombinant human lactoferrin (rhLF) expressed in the milk of transgenic mice with natural human milk-derived lactoferrin (hLF). They concluded that the unsaturated rhLF and natural hLF had comparable properties, indicating that hLF produced in bovine milk will exert similar, if not identical, antibacterial and anti-inflammatory activities in vivo. Pharming also developed the first transgenic bull in the late... 

Law, B. A, and Reiter, B, (1977) The isolation and bacteriostatic properties of lactoferrin from bovine milk whey. 

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