Abstract
Iron plays an important role in cell growth and metabolism, and as many key reactions in energy metabolism and DNA synthesis are catalyzed by iron-containing enzymes, some biologists have considered it likely that iron was an obligatory requirement during the earliest phases of the evolution of life (Shapira, 1964; Neilands, 1972). Under most physiological conditions, however, the iron atom exists in its oxidized ferric (Fe3+) state and at neutral pH ferric salts are hydrolyzed to insoluble ferric hydroxide. Thus ferric ions in excess of 2.5 × 10–18 M are insoluble. To combat this problem, organisms have developed various systems to maintain iron in a soluble form and transport it into the cell. Micro-organisms have solved this problem by producing and secreting various soluble iron-chelating molecules referred to as siderophores (Neilands, 1981) whereas vertebrates have developed a family of closely related iron-binding proteins collectively known as the transferrins (Aisen and Listowsky, 1980).
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Trowbridge, I.S., Newman, R.A. (1984). Monoclonal Antibodies to Transferrin Receptors. In: Greaves, M.F. (eds) Monoclonal Antibodies to Receptors. Receptors and Recognition, vol 17. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-5566-0_10
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DOI: https://doi.org/10.1007/978-94-009-5566-0_10
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