Milk, lactoferrin

Rainard, P. 1986. Bacteriostatic activity of bovine milk lactoferrin against mastitic bacteria. Vet. Microbiol. 11, 387-392. 

The recombinant whole molecules are both expressed in glycosylated form, although the glycosylation patterns differ from the proteins isolated from natural sources. The recombinant human transferrin binds to receptors both in its glycosylated form and as a nonglycosylated mutant, showing that the carbohydrate is not required for receptor binding (230). Recombinant human lactoferrin shows identical spectroscopic properties and shows an identical profile of pH-dependent iron release when compared with human milk lactoferrin (231). 

Glycoproteins, bovine whey. See Glycoproteins Glycoproteins, iron-binding, milk, lactoferrin. See Lactoferrin Glycosaminoglycans... 

Lactoferrin contents rise dramatically in the milks of mastitic cattle. This apparently represents a normal physiological defense mechanism similar to the nutritional immunity discussed in a previous section, except that here not only the UIBC but also TIBC-values of the milks increase drastically. In such milks, lactoferrin values may be as high as 6 mg/ml, lactoferrin thus becoming a major milk protein component. It is apparently synthesized by the epithelial cells rather than being released by the neutrophils that are also present in such milks (Harmon et al., 1976), The function of the transferrins in other types of infections in cattle have not yet received much attention, and should represent a fertile area for future research activity. 

Iron is, as part of several proteins, such as hemoglobin, essential for vertebrates. The element is not available as ion but mostly as the protein ligands transferrin (transport), lactoferrin (milk), and ferritin (storage), and cytochromes (electron transport) (Alexander 1994). Toxicity due to excessive iron absorption caused by genetic abnormalities exists. For the determination of serum Fe a spectrophoto-metric reference procedure exists. Urine Fe can be determined by graphite furnace (GF)-AAS, and tissue iron by GF-AAS and SS-AAS (Alexander 1994 Herber 1994a). Total Iron Binding Capacity is determined by fuUy saturated transferrin with Fe(III), but is nowadays mostly replaced by immunochemical determination of transferrin and ferritin. 

Van Berkel, P.H., Welling, M.M., Geerts, M. et al. (2002) Large scale production of recombinant human lactoferrin in the milk of transgenic cows. Nature Biotechnology, 20 (5), 484—487. 

Research is under way to investigate the potential to develop the natural antimicrobial system present in milk, such as the lysozyme, lactoferrin,... 

So called because they are found in milk, where the iron-binding protein lactoferrin sequesters iron so tightly... 

NHH Heegaard, J Brimnes. Comparison of heparin binding to lactoferrin from human milk and from human granulocytes by means of affinity capillary electrophoresis. Electrophoresis 17 1916-1920, 1996. 

Lactoferrin is the major whey protein present in breast milk (Teraguchi et ah, 1996) with many microbicidal properties (Leon-Sicairos et ah, 2006). The concentration of lactoferrin in milk has been reported as 1 g/liter in mature milk and 7 g/liter in colostrum (Houghton et ah, 1985). The concentration of lactoferrin in breast milk is controlled by the reproductive hormones prolactin and estrogen (Ward et ah, 2005). Lactoferrin has been demonstrated to resist digestion in the infant gut as it has been recovered intact from the stool of breast-fed infants (Bemt and Walker, 1999). Lactoferrin acts mainly in an iron-free state (apo-lactoferrin) and its microbicidal activity is reported to increase in proportion to its concentration in milk (Leon-Sicairos et ah, 2006). 

It has been suggested that lactoferrin may only confer beneficial immune effects when consumed in the form of breast milk (Lonnerdal, 2003). When added to infant formula, lactoferrin may be affected by its prior bioactivity how it was added (blended or dissolved) and extent of heat treatment of the formula (Lonnerdal, 2003). There is evidence that lactoferrin can be inactivated by invading pathogens or even enhance microbial pathogenicity. For example, the pneumococcal surface protein A of Streptococcus pneumoniae was reported to bind to lactoferrin and protect the bacteria from the killing action of lactoferrin (Ward et ah, 2005). 

Houghton, M., Santoso, H., Soetjiningsih, and Gracey, M. (1985). Lactoferrin concentrations in the breast milk of Indonesian mothers. Paediatr. Indones. 25,163-166. 

Leon-Sicairos, N., Lopez-Soto, F., Reyes-Lopez, M., Godinez-Vargas, D., Ordaz-Pichardo, C., and de la, G. M. (2006). Amoebicidal activity of milk, apo-lactoferrin, sIgA and lysozyme. Clin. Med. Res. 4,106-113. 

Butler, J. E. 1973. The occurrence of immunoglobulin fragments, two types of lactoferrin and a lactoferrin-IgG2 complex in bovine colostral and milk whey. Biochim. Bio-phys. Acta 295, 341-351. 

Senft, B. and Klobasa, F. 1973. Research on the concentration of lactoferrin in colostral and ripe milk from cows. Milchwissenschaft 28, 750-752 (German). 

Microbial inhibitors in raw milk include lactoferrin, lysozyme, the lac-toperoxidase/thiocyanate/hydrogen peroxide system, specific immuno-... 

Masson, P. L. and Heremans, J. R. 1971. Lactoferrin in milk from different species. Comp. Biochem. Physiol. 39B, 119-129. 

The transferrins are proteins that bind and transport iron as peIII 16-U.8 They indude lactoferrin from milk, ovotransferrin from egg white, and serum transferrin from a range of organisms. Uteroferrin, considered in Section 62.1.5.5.2 on the purple acid phosphatases, is an iron-binding protein with phosphatase activity, that has been proposed to transport iron from maternal to foetal circulation.824 826 There are distinct differences between the iron-binding sites in uteroferrin and transferrin, and so uteroferrin will not be discussed in this section. 

Lactoferrin occurs in high concentrations in human milk. It has high affinity for iron, and it may have a bacteriostatic function in depriving microbes of essential iron required for their growth. It supplies iron to intestinal tissue and probably has a nutritional role in supplying iron to newly born infants. 

Mother s milk is an often coined term for products that mimic the natural mother s milk contents. Actual human mother s milk contains about 40-50% casein and 50-60% whey, and about 17% lactoferrin with no beta-lactoglobulin. As I said earlier, mother s milk contains alfa lactoglobulin. This is very different from cow s milk which contains about 80% casein and 20% whey with 1% lactoferrin being average. Lactoferrin has anti-viral activity, and is a potent immune system booster. Obviously this is an advantage for new born human (rug rats) since they lack complete immune system functions. Remember the fact that human mother s milk dominant protein fraction is alfa-lactalbumin Well, there is a research project on going which claims acid folded alfa-... 

---