Studies on the Binding of Iron to Transferrin and Conalbumin

Electrophoretic studies of the binding of iron to transferrin indicate that the stability constants of the two binding sites are approximately equal. The iron in each site also acts independently in relaxing the protons of the solvent water. It appears likely, then, that the binding sites are equivalent and independent. Similar results have been obtained for conalbumin, corroborating the evidence that the two proteins have similar structure.