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- W2410301455 endingPage "43" @default.
- W2410301455 startingPage "31" @default.
- W2410301455 abstract "Brock, J. H. (Department of Bacteriology and Immunology, Western Infirmary, Glasgow, UK). Iron-binding proteins. The structure and properties of the iron-binding proteins transferrin, lactoferrin and transferrin are reviewed. Transferrin and lactoferrin are structurally similar, consisting of a single polypetide chain and reversibly binding two iron atoms per molecule. Transferrin is found mainly in serum, whereas lactoferrin is found in neutrophils and in external secretions. Transferrin functions mainly as a donor of iron to cells, but there is no established iron-transport role for lactoferrin. Both these proteins may have antimicrobial activity as a result of their ability to sequester iron. Lactoferrin may act principally as a scavenger of iron in conditions where transferrin may not bind iron well, e.g. at low pH. Ferritin is a multisubunit protein capable of binding up to 4 000 iron atoms and serves principally as an iron-storage protein, though it may also serve to detoxify iron. In iron-rich tissues ferritin is largely degraded and the iron is converted to haemosiderin." @default.
- W2410301455 created "2016-06-24" @default.
- W2410301455 creator A5018216805 @default.
- W2410301455 date "1989-10-01" @default.
- W2410301455 modified "2023-09-29" @default.
- W2410301455 title "Iron-binding Proteins" @default.
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