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Lactotransferrin - function, effect & structure explained
Lactotransferrin is an iron-binding protein with immune-strengthening, antimicrobial and anti-inflammatory effects.
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Lactotransferrin is an iron-binding protein that plays an important role in iron metabolism and immune defence.
Lactotransferrin (Latin: lacteus = milk, ferrum = iron and transferre = transfer) is also known as lactoferrin. Lactoferrin belongs to the protein family of transferrins. It is found in body fluids such as saliva, tears and breast milk and helps to inhibit the growth of bacteria by binding iron. In addition, lactoferrin / lactotransferrin has anti-inflammatory, antioxidant and antimicrobial properties, making it a valuable nutrient for supporting the immune system. It is also used to treat iron deficiency and iron deficiency anaemia, as it can promote iron absorption in the body.
Lactoferrin is a protein that consists of a polypeptide chain with around 700 amino acids and forms two globular domains, the N-lobe and C-lobe. These domains bind metal ions such as iron, zinc or copper. Lactoferrin has an affinity for iron that is around 300 times higher than transferrin and is divided into two forms: iron-rich hololactoferrin and iron-free apolactoferrin. It plays an important role in immune defence and iron metabolism, whereby its molecular weight varies between 76 and 80 kDa depending on the glycosylation.
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