Competitive advantage of diferric transferrin in delivering iron to reticulocytes.

Abstract
Radioiron- and radioiodine-labeled forms of human diferric and monoferric transferrin and apotransferrin, isolated by preparative isoelectric focusing, were used to define transferrin-Fe uptake by human reticulocytes. In mixtures of human diferric and monoferric transferrin, the diferric molecule had a constant 7-fold advantage in delivering Fe to reticulocytes, as compared with the 2-fold advantage when single solutions of mono- and diferric transferrins were compared. This was due to competitive interaction in Fe delivery, probably at a common membrane-receptor binding site for transferrin. Apotransferrin did not interfere with the Fe-donating process and its limited cellular uptake was inhibited in noncompetitive fashion by diferric transferrin.

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