Lactoferrin is a protein belonging to the iron transporter family that occurs naturally in several bodily fluids such as tears, saliva,mucus and milk. Found in mother's milk produced 24 to 48 hours after birthing, lactoferrin provides the body's first immune defense. Colostrum, in lactoferrin is the pre-milk fluid produced by mammals immediately after birthing. With high protein, immunoglobulin, it's nature's perfect food contributing to newborn's defense system. Adult supplementation shows promise for health-promoting benefits. Lysozyme, an enzyme in lactoferrin, is a natural antagonist to harmful invaders. Lysozyme joins forces with other lactoferrin benefits to exert powerful immune activity. Lactoferrin Plus contains compounds naturally occurring in the body. It is a 100% natural product, allergy free with no side effects or drug interactions. Lactoferrin is an 80kD globular protein found in milk and many mucosal secretions such as tears.
Lactoferrin is a glycoprotein belonging to the transferrin family of iron-transport proteins. Like transferrin, lactoferrin is a single-chain protein with a molecular weight of ~80Kda, folded into two lobes, each of which can reversibly bind one ferric ion (Fe3+). Two biochemical features distinguish lactoferrin from transferrin: firstly, lactoferrin is a highly basic protein with a pI of ~8, whereas transferrin has a pI of 5.5-6.0; secondly, transferrin releases its bound iron at pH ~5 whereas lactoferrin can retain its iron to around pH3.0 or lower. In addition, the two proteins have quite different distributions, transferrin being essentially a protein of plasma and extravascular fluid, whereas lactoferrin is found in the secondary granules of neutrophils and in external secretions, notably breast milk. The neutrophil and secretory forms of lactoferrin are identical except for their glycan chains, and there appear to be no other structural or functional differences between them.
Lactoferrin is a glycoprotein that belongs to the iron transporter or transferrin family. It was originally isolated from bovine milk, where it is found as a minor protein component of whey proteins (see Whey Proteins). Lactoferrin contains 703 amino acids and has a molecular weight of 80 kilodaltons. In addition to its presence in milk, it is also found in exocrine secretions of mammals and is released from neutrophil granules during inflammation.
Lactoferrin is considered a multifunctional or multi-tasking protein. It appears to play several biological roles. Owing to its iron-binding properties, lactoferrin is thought to play a role in iron uptake by the intestinal mucosa of the suckling neonate. That is, it appears to be the source of iron for breast-fed infants. It also appears to have antibacterial, antiviral, antifungal, anti-inflammatory, antioxidant and immunomodulatory activities. Three isoforms of lactoferrin have been isolated: lactoferrin-alpha, lactoferrin-beta and lactoferrin-gamma. Lactoferrin-beta and lactoferrin-gamma have RNase activity, whereas lactoferrin-alpha does not. Receptors for lactoferrin are found in monocytes, lymphocytes, neutrophils, intestinal tissue and on certain bacteria. Lactoferrin is abbreviated LF and Lf. Bovine lactoferrin is abbreviated bLF.
The possible antibacterial activity of supplemental lactoferrin might be accounted for, in part, by its ability to strongly bind iron. Iron is essential to support the growth of pathogenic bacteria. Lactoferrin may also inhibit the attachment of bacteria to the intestinal wall. A breakdown product of lactoferrin is the peptide lactoferricin. Lactoferricin, classified as a bioactive peptide, may also have antibacterial, as well as antiviral, activity. The possible antiviral activity of supplemental lactoferrin may be due to its inhibition of virus-cell fusion and viral entry into cells. A few mechanisms are proposed for lactoferrin's possible immunomodulatory activity. Lactoferrin may promote the growth and differentiation of T lymphocytes. Lactoferrin appears to bind uniquely in the region of major histocompatability (MHC) proteins and the CD4 and CD8 determinants on T4 (helper) and T8 (suppressor) lymphocytes; it bears sequence homologies with the MHC Class II determinant. Lactoferrin also appears to play a role in the regulation of cytokines and lymphokines, such as tumor necrosis (TNF)-alpha and interleukin (IL)-6. Lactoferrin's possible antioxidant activity may also contribute to its possible immunomodulatory activity. Lactoferrin's possible antioxidant activity can also be accounted for by its ability to strongly bind iron. Free iron is a major contributor to the generation of reactive oxygen species via the Fenton reaction.