Abstract
When radioiron-labelled transferrin with 55Fe located predominantly in the N-terminal iron-binding site and 59Fe predominantly in the C-terminal iron-binding site was incubated with rabbit reticulocytes, both radioisotopes of iron were removed at similar rates. Electrophoresis of transferrin samples taken during the course of an incubation, in polyacrylamide gels containing 6 M-urea, showed that iron was removed in a pairwise fashion, giving rise to iron-free transferrin.