Iron exchange between ferritin and transferrin in vitro.
The transfer of iron between horse spleen [55Fe]ferritin and human apotransferrin or [59Fe]transferrin in homogeneous solution was investigated. Transfer between the two proteins in the presence of citrate, ATP, or ascorbate occurs in both direction, but the net flow is always from ferritin to transferrin. Ferritin which is ca. 1/3 to 1/2 saturated with iron appears to be most reactive. Chemically prepared apoferritin does not accept iron from diferric transferrin. Citrate-mediated transfer of iron from ferritin to apotransferrin is first order with respect to ferritin, zero order with respect to transferrin, and has a complex dependence upon citrate concentration. Direct transfer of iron from native or reconstituted ferritin to apotransferrin in the absence of any identifiable mediating agent was observed to occur at about half the rate attained in the presence of 1 mM citrate. No transfer of iron between the two proteins occurs across a dialysis membrane in the absence of a mediating agent. No binding of transferrin and ferritin to each other was demonstrable. One possible explanation for these observations is that iron from the core of ferritin is in equilibrium with iron near the outer surface of the protein, where the metal would be available to transferrin.
D000818:Animals; D001059:Apoproteins; D005293:Ferritins; D006736:Horses; D006801:Humans; D007501:Iron; D007700:Kinetics; D011485:Protein Binding; D013154:Spleen; D014168:Transferrin / Q000097:blood
D001059:Apoproteins; D014168:Transferrin; D005293:Ferritins; D007501:Iron