The biology of lactoferrin
Structure, iron binding, and the mechanisms that are genuinely established rather than merely proposed.
Lactoferrin is a single polypeptide chain of roughly 80 kilodaltons, folded into two globular lobes of similar architecture. Each lobe carries a binding site that holds one ferric iron ion, together with a carbonate ion, and holds it far more tightly than the related serum protein transferrin does.
That binding is the origin of most of what the protein is known for. It is also the origin of its two visible states: iron-free lactoferrin is colorless, while the iron-saturated form carries a distinct salmon color, which is why early literature referred to the red protein of milk.
Pages here cover the structure, the binding chemistry, where the protein is produced and released, and which of the proposed mechanisms have support beyond a single laboratory.
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This page reports published research. It is general information, not medical advice, and not a recommendation to take anything. Lactoferrin supplements are derived from cow's milk and are unsuitable for anyone with a milk protein allergy. Anyone who is pregnant, breastfeeding, treating an infant, or managing a diagnosed condition should speak to a clinician first.