Chelation and Iron Metabolism I. Relative Iron Binding of Chelating Agents and Siderophilin in Serum.

Abstract

A series of synthetic amino acid chelating agents of a graded order of Fe binding strength was tested for its ability to donate, remove, or competitively bind Fe in the presence of Fe binding protein in rabbit serum. Weakly complexed Fe of the glycine derived chelates donated the metal to protein. None of the chelates could remove Fe from the protein. The more potent Fe binding chelates of the ethylene diamine structure were able to compete with protein for added Fe with an efficiency dependent on the intrinsic Fe binding ability of the individual chelate.