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In vitro-studies show that the Ca-chelates of EDTA and DTPA are equally effective in removing Zn from the proteins and that the Zn-protein pool is composed of several fractions with different stabilities. Only a small fraction of the protein-bound Zn can be labelled by  65 Zn in vitro and, as to the mobilization of  65 Zn, Ca-DTPA was found to be 20 times more effective than equimolar Ca-EDTA. The isotope exchange between Zn-DTPA and protein-bound  65 Zn is an extremely fast reaction whereas in the case of Zn-EDTA a sluggish exchange takes place. The analysis of the results led to conclusion that the ligand and isotope exchange reactions in the case of EDTA proceed via the free Zn 2+ -ion; with the high-dentate DTPA, however, the formation of ternary and mixed complexes plays an important role. The implications of the findings as related to the toxicity of the Ca-chelates are discussed.

zeitschrift für naturforschung b

Liganden- und Isotopenaustausch im System: Serumproteine — Zink — Polyaminopolycarbonsäuren / Ligand and Isotope Exchange in the System: Serum Proteins — Zinc — Polyaminopolycarbonic Acids