Tag: Iron binding

Lactoferrin, a glycoprotein found in milk and other bodily fluids, is capable of binding two ferric iron ($Fe^{3+}$) ions per molecule. The specific iron saturation level of lactoferrin is not a fixed value but exists along a continuum, dictating its stability and function in the body.

Lactoferrin was first isolated from cow's milk in 1939, and later discovered to be a crucial multifunctional protein in human milk and other bodily fluids. In its natural, unaltered form, known as native lactoferrin, this glycoprotein maintains its full biological activity, offering unique advantages for immune support and iron metabolism.

According to the National Institutes of Health, lactoferrin is a major component of the mammalian innate immune system and is found in milk. The concentration of lactoferrin in a glass of milk varies drastically depending on the species and the stage of lactation, revealing significant differences in this beneficial protein.

Lactoferrin, a multifunctional iron-binding glycoprotein, is found in various mammalian body fluids, including milk, saliva, and tears. This powerful protein has several other names, with one of the most prominent being lactotransferrin. The different names reflect its key characteristics and functions within the body, which play crucial roles in host defense and overall health.

Lactoferrin, a multifunctional glycoprotein, was first isolated from bovine milk in 1939. This vital protein is not just a simple component of milk but is an active agent composed of a complex structure that confers numerous health-promoting effects, including robust immune system support. Lactoferrin's rich composition is key to understanding its powerful and versatile role in human nutrition and health.