[Effect of pH and the binding anion on In3+-transferrin interaction: spectroscopic study of the perturbed angular correlation of 172-245 keV gamma rays of indium 111].

The formation of ternary complexes, transferrin-anion-In111 has been investigated by means of gamma-gamma coincidence spectrometry of the 172-245 keV rays. The angular correlation between the two gamma-rays emitted in cascade depends on the magnetic and electric fields gradients, consequently the chemical structure of metal holder. Any modification of this structure causes the variation of angular correlation. The study of G22 (infinity) as function of pH (G22(infinity): integrated perturbed angular correlation coefficient) has been performed to turn out the hydrolysis of In111 in aqueous solution, metal complex formation in presence of chelating agents (citric acid and sodium bicarbonate) and the formation of protein-metal complexes. The presence of complexing agents limits the domain of In111 colloid existence and allows fast transfer of ionised indium on the transferrin. Two types of metal-protein interactions has been turn out. The first in the weakly acidic range of pH is characterized by an affinity constant near to this of citric acid. The second lying in neutral and basic range of pH, where the formation rate of transferrin-In111 complex is fast (t less than 500 s). In citrate medium, for pH 6-7,5 the rate of metal transfer on the protein, studied by means of G22 (infinity) = f(t), is function of pH. The binding anion appears as an indispensable element for the formation of protein-metal complexes. The In111 previously chelated by 8-Hydroxyquinoline is fixed by the protein if only exits a binding anion in the solution. This mays bring in the formation of an intermediate active state, indispensable step for the ternary complex formation transferrin-anion-In111.