[The mechanisms of the interaction of contrast media with serum albumin and gamma-globulin studied by means of fluorescence extinction and equilibrium dialysis].

The mechanisms binding X-ray contrast media and magneto-resonance contrast media of various structure with human serum albumin and gamma-globulins were studied. Equilibrium dialysis showed that X-ray contrast media bind with blood plasma proteins, but magneto-resonance contrast media do not interact with these proteins. Electrostatic forces play a significant role in formation of complexes of X-ray contrast media with human blood serum albumin. With increase in the size of the molecule of the X-ray contrast media their affinity for the binding sites of this protein diminishes. The formation of complexes of X-ray contrast media with human blood plasma gamma-globulins occurs through hydrophobic interactions. Increase in the size of the molecules of these media reduces their affinity for the gamma-globulin binding sites.