[Study of interaction between contrast media and human serum albumin by the fluorescence method]

Structural changes in the human serumal albumin under the effect of roentgen-contrast media, viz. bilignost, triiotrast, endografine, iodamide, triombrine and cardiotrast, were investigated by the method of fluorescence. The complex-formation of albumin with triiodotrast, bilignost and endografine was shown to call forth a short-wave shift of the fluorescence peak by approximately 20 nm. The binding section for these substances is characterized by an association constant equalling 1.2-10(5) M-1. The authors presume that triiodotrast, bilignost and endografine cause changes in the microstructure of the aqueo-protein layer in the area of the tryptophan residue localization. As to triombine, iodamide and cardiotrast fluorescence failed to disclose their combination with the human serumal albumin.