Abstract
Although the presence in blood serum of iron which was not part of heme, and was neither ultrafiltrable nor dialyzable, was recognized almost 50 years ago (Katz, 1970), the precise physicochemical nature of this iron-bearing component was established only after the development of reliable procedures for the fractionation of blood proteins. In 1945 Holmberg and Laurell in Sweden established the existence of an iron-transporting protein in blood which they punningly named transferrin (Holmberg and Laurell, 1945, 1947). Almost simultaneously Schade and Caroline (1946) in the United States demonstrated that the bacteriostatic activity of blood plasma was in part due to a protein with an enormous avidity for iron which they therefore named siderophilin. These investigators further established the remarkable similarity of the iron-complexing properties of the blood protein to those of conalbumin, a protein present in egg white (1944). Because of this similarity, the designation ovotransferrin for the egg protein is currently gaining widespread usage (Feeney and Komatsu, 1966). Finally, a “red protein” from milk has also been shown to display the same type of iron-binding activity as transferrin and conalbumin, and hence has been given the name lactoferrin (Masson and Heremans, 1967, 1968). This is something of a misnomer, since lactoferrin occurs in a variety of physiological fluids as well as in leucocytes. Together, serum transferrin, conalbumin (ovotransferrin) and lactoferrin comprise the class of proteins often designated as “the transferrins” (Feeney and Komatsu, 1966).
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© 1974 Plenum Press, New York
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Aisen, P., Leibman, A., Pinkowitz, R.A. (1974). The Anion-Binding Functions of Transferrin. In: Friedman, M. (eds) Protein-Metal Interactions. Advances in Experimental Medicine and Biology, vol 48. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-0943-7_7
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DOI: https://doi.org/10.1007/978-1-4684-0943-7_7
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