title: [Binding of 67 Ga and 59 Fe to ferritin or transferrin].
abstract: The bindings of 67Ga and 59Fe to ferritin or transferrin in vitro has been investigated. Affinity constants have been measured using the equilibrium dialysis, and the results have been obtained as follows: 1 Apo-ferritin could not bind to 67Ga until it was transformed into ferritin in presence of Fe-citrate. On the contrary, the affinity of 67Ga to ferritin was reduced when Fe was released from ferritin; thus indicating that Fe-core has been required for the binding of 67Ga to ferritin. 2 Binding of 67Ga to ferritin was inhibited with apo-transferrin, and this was also shown in the case of 59Fe. In the presence of NaHCO3 or citrate, more remarkable inhibitions were observed. NaHCO3 or citrate was found to give a synergistic effect on the binding of 67Ga to transferrin, as well as Fe-transferrin. Therefore, both 67Ga and 59Fe could not bind to ferritin in the state of 67Ga- or 59Fe-transferrin. 3 The release of 59Fe from 59Fe-transferrin was enhanced with adenosine triphosphate (ATP), citrate, or ascorbic acid, while any of these reagents did not affect the release of 67Ga from 67Ga-transferrin. The comparison of 59Fe and 67Ga through their bindings to ferritin or transferrin has suggested one of points to distinguish 67Ga from 59Fe in the cell.
mesh_terms: D001052:Apoferritins; D001667:Binding, Competitive; D005293:Ferritins; D005710:Gallium Radioisotopes; D007504:Iron Radioisotopes; D011485:Protein Binding; D014168:Transferrin
chemical_list: D005710:Gallium Radioisotopes; D007504:Iron Radioisotopes; D014168:Transferrin; D005293:Ferritins; D001052:Apoferritins