Higher levels of lactoferrin in the human body are found in colostrum, (3.1-6.7 mg/ml), in breast milk (1.0-3.2 mg/ml), and in blood (0.02-1.52 μg/ml).
Levay P.F., Viljoen M. (1995): Lactoferrin: a general review. Haematologica, 80, 252–267.
The ability of lactoferrin to combine with iron ions or molecules is twice as high as that of other proteins of the transferrin family (serum transferrin, ovotransferrin, and melanotransferrin).
Aisen P., Liebman A. (1972): Lactoferrin and transferrin: a comparative study. Biochimica et Biophysica Acta, 257, 314–323.
Not only is lactoferrin able to combine with iron ions or molecules (Fe3+), but it can also combine with many compounds and substances, such as lipopolysaccharides, heparin, glycosaminoglycans, and other metallic ions such as zinc (Zn2+), copper (Cu2+), aluminium (Al3+), manganese (Mn3+), cobalt (Co3+), etc.
Baker E.N. (1994): Structure and reactivity of transferrins. Advances in Inorganic Chemistry, 41, 389–463.
Lactoferrin is the second most abundant milk protein, after casein.
Connely OM. Antiinflammatory activities of lactoferrin. J Am Coll Nutr 2001;20(5 Suppl.):389S–95S.
Lactoferrin was first isolated in 1939 from cow's milk and in 1960 from human milk.
Sorensen M., Sorensen S.P.L. (1939): The proteins in whey. Comptes-rendus des Travaux du Laboratoire Carlsberg, 23, 55–99. Lönnerdal B., Iyer S. 1995. Lactoferrin: molecular structure and biological function. Annual Reviews of Nutrition, 15(7): 93-110.
There are three types of lactoferrin depending on whether they are combined with iron molecules: apolactoferrin (iron-free), monoferric or partial form (combined with one iron molecule) and hololactoferrin (combined with two iron molecules).
Jameson GB., Anderson BF., Norriss G.E., Thomas D.H., Baker E.N. (1998): Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallographica. Section D, Biological Crystallography, 54, 1319–1335.