Bovine lactoferrin

Weiner, R. E. and Szuchel, S. 1975. The molecular weight of bovine lactoferrin. Biochim, Biophys. Acta 393, 143-147. 

Paulsson, M.A., Svensson, U., Kishore, A.R., andNaidu, A.S. 1993. Thermal behavior of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity. J Dairy Sci 76(12) 3711-3720. 

Zheng, J., Ather, J.L., Sonstegard, T.S., and Kerr, D.E. 2005. Characterization of the infection-responsive bovine lactoferrin promoter. Gene 353(1) 107—117. 

Puddu, P., Borghi, P., Gessani, S., Valenti, P., Belardelli, F., and Seganti, L. 1998. Antiviral activity of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection. Int. J. Biochem. Cell Biol. 30, 1055-1063. 

Bellamy, W.R., Takase, M., Wakabayashi, H., Kawase, K., and Tomita, M. 1992a. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal of bovine lactoferrin. J. Appl. Bacteriol. 73, 472-479. 

Debbabi, H., Dubarry, M., Rautureau, M., and Tome, D. 1998. Bovine lactoferrin induces both mucosal and systemic immune responses in mice. J. Dairy Res. 65, 283-293. 

Dionysius, D.A. and Milne, J.M. 1997. Antibacterial peptides of bovine lactoferrin purification and characterization. J. Dairy Sci. 80, 667-674. 

Hoek, K.S., Milne, J.M., Grieve, P.A., Dionysius, D.A., and Smith, R. 1997. Antibacterial activity of bovine lactoferrin-derived peptides. Antimicrob. Agents Chemother. 41, 54-59. 

Roberts, A.K., Chierici, R., Sawatzki, G., Hill, M.J., Volpato, S., and Vigi, V. 1992. Supplementation of an adapted formula with bovine lactoferrin 1. Effect on the infant faecal flora. Acta Paediatr. 81, 119-124. 

Sekine, K., Ushida, Y., Kuhara, T., Iigo, M., Baba-toriyama, H., Moore, M.A., Murakoshi, M., Satomi, Y.M., Nishino, H., Kakizoe, T., and Tsuda, H. 1997. Inhibition of initiation and early stage development of aberrant crypt foci and enhanced natural killer activity in male rats administered bovine lactoferrin concomitantly with azoxymethane. Cancer Lett. 121, 211—216. 

Siciliano, R., Rega, B., Marchetti, M., Seganti, L., Antonini, G., and Valenti, P. 1999. Bovine lactoferrin peptidic fractions involved in inhibition of herpes simplex virus type I infection. Biochem. Biophys. Res. Commun. 264, 19—23. 

Teraguchi, S., Shin, K., Ogata, T., Kingaku, M., Kaino, A., Miyauchi, H., Fukuwatari, Y., and Shimamura, S. 1995a. Orally administered bovine lactoferrin inhibits bacterial translocation in mice fed bovine milk. Appl. Environ. Microb. 61, 4131-4134. 

Tsuda, H., Sekine, K., Fujita, K.I., and Iigo, M. 2002. Cancer prevention by bovine lactoferrin and underlying mechanisms—a review of experimental and clinical studies. Biochem. Cell Biol. 80, 131-136. 

Wada, T., Aiba, Y., Shimizu, K., Takagi, A., Miwa, T., and Koga, Y. 1999. The therapeutic effect of bovine lactoferrin in the host infected with Helicobacter pylori. Scand. J. Gastroenterol. 34, 238-243. 

Bihel, S., Birlouez-Aragon, I. 1998. Inhibition of tryptophan oxidation in the presence of iron-vitamin C by bovine lactoferrin. Int. Dairy J. 8, 637-641. 

Fig. 4. Ribbon diagram of human diferric lactoferrin, showing the organization of the molecule, with the N-lobe above and C-lobe below. The four domains (Nl, N2, Cl, C2), the interlobe connecting peptide (H), and the C-terminal helix (C) are indicated. The glycosylation sites in various transferrins are shown by triangles and numbered (1, human transferrin 2, rabbit transferrin 3, human lactoferrin 4, bovine lactoferrin 5 chicken ovotransferrin). The interdomain backbone strands in each lobe can be seen behind the iron atoms. Adapted from Baker et al. (82), with permission.

A final point of general organization concerns the carbohydrate. All transferrins so far characterized, except apparently for one fish transferrin (84), are glycoproteins. There is, however, no pattern to the sites of attachment of the carbohydrate chains on different proteins—they appear almost randomly distributed over the protein surface (Fig. 4), strengthening the view that the carbohydrate plays no direct role in function. Rabbit serum transferrin, for example, has one carbohydrate chain, on its C-lobe (residue 490) human serum transferrin has two, both on the C-lobe (residues 416 and 611) human lactoferrin has two, one on each lobe (at residues 137 and 478) and bovine lactoferrin has four, one on the N-lobe (residue 233) and three on the C-lobe (residues 368, 476, and 545). 

Human transferrin Rabbit transferrin Pig transferrin Horse transferrin Human lactoferrin Mouse lactoferrin Bovine lactoferrin Pig lactoferrin Chicken ovotransferrin Xenopus transferrin Cockroach transferrin M. sexta transferrin Melanotransferrin... 

Tomita M, Wakabayashi H, Yamauchi K, Teraguchi S, Hayasawa H (2002) Bovine lactoferrin and lactoferricin derived from milk production and applications. Biochem Cell Biol 80 109-112 Tsuge T, Tanaka K, Ishizaki A (2001) Development of a novel method for feeding a mixture of L-lactic acid and acetic in fed-batch culture of Ralstonia eutropha for poly-D-3-hydroxybu-tyrate production. J Biosci Bioeng 91 545-550... 

Xavier et al. have reported the AU25 core protected with native (bovine) lactoferrin. They have also identified the intermediate Au g core from the MALDI MS data. They have extended their study to see the evolution of clusters where they have shown that gold ions organize to create the cluster core through aurophillic interactions leading to regeneration of the free protein. We ll discuss this in detail in the following sub-section. 

Lactoferrin is a glycoprotein found in mammalian milk that tightly binds two ferric ions producing an iron complex more physically and chemically stable than the uncomplexed protein. Bovine lactoferrin inhibited oxidation in com oil-in-water emulsions and lecithin liposome systems (Table 10.8). At the same molar concentration, lactoferrin was less effective than EDTA in inhibiting hydroperoxide formation in a com oil emulsion. This lower antioxidant activity of lactoferrin may be explained by its partial iron saturation and lower affinity for ferric ions. The formation constant for ferric-EDTA is 1.3 x 10 compared to 10 ° for the ferric-lactoferrin complex. Lactoferrin was a better iron chelator in the liposome than in the emulsion systems. Inhibition in liposomes with iron-lactoferrin mixtures was in the order 1 2 > 1 1 > 2 1. This order suggested that lactoferrin also chelated metal impurities as well as added iron to inhibit lipid oxidation. Lactoferrin did not inhibit the copper-catalysed... 

Iron supplementation to meet nutritional requirements can seriously limit the shelf life of milk products especially infant formulas. lipid oxidation can be controlled in iron-supplemented milk by using lactoferrin, a non-heme ironbinding glycoprotein found in human (1.4 mg/ml) and bovine milk (0.1 mg/ ml). Lactoferrin in bovine milk is 22% saturated with iron compared to 4% in mature human milk. Compared to human milk, infant formulas are more susceptible to lipid oxidation because they are supplemented with greater amounts of iron and do not contain lactoferrin. This antioxidant protein in milk has an important activity by binding prooxidant iron ions. Commercially available bovine lactoferrin, isolated from cheese whey, inhibited lipid... 

Moore SA, Anderson BF, Groom CR et al (1997) Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolutirat. J Mol Biol 274(2) 222-236... 

Antonini G, Rossi P, Pitari G et al (2000) Role of glycan in bovine lactoferrin. In Shimakaki K, Tsuda H, Tomita M, Kuwata T, Perraudin JP (eds) Lactoferrin structure, frmetion and applications. Elsevier Science, Amsterdam, pp 3—16... 

Rossi P, Giansanti F, Boffi A et al (2002) Ca Binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide. Biochem Cell Biol 80 41 8... 

Lampreave F, Pineiro A, Brock JFI et al (1990) Interaction of bovine lactoferrin with other proteins of milk whey. Int J Biol Macromol 12(l) 2-5... 

Y. Nojima, K. Iguchi, Y. Suzuki, A. Sato, The pH-dependent formation of PEGylated bovine lactoferrin by branched polyethylene glycol (PEG)-N-hydroxysuccinimide (NHS) active esters. Biol. Pharm. Bull, 32 (3) 523-526,2009. 

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