[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.
Shabunin
I V
IV
Panov
V O
VO
Kalinina
A A
AA
Shimanovskiĭ
N L
NL
Sergeev
P V
PV
D003287:Contrast Media / Q000032:analysis / Q000493:pharmacokinetics / Q000494:pharmacology*; D003956:Dialysis / Q000379:methods / Q000706:statistics & numerical data; D004305:Dose-Response Relationship, Drug; D004347:Drug Interactions; D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding / Q000187:drug effects; D012709:Serum Albumin / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence / Q000379:methods / Q000706:statistics & numerical data; D013329:Structure-Activity Relationship; D005719:gamma-Globulins / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology*
D003287:Contrast Media; D012709:Serum Albumin; D005719:gamma-Globulins