Shabunin I V, Panov V O, Kalinina A A, Shimanovskiĭ N L, Sergeev P V
Eksp Klin Farmakol. 1996 Sep-Oct;59(5):43-6.
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.
研究了各种结构的X射线造影剂和磁共振造影剂与人血清白蛋白和γ-球蛋白的结合机制。平衡透析表明，X射线造影剂与血浆蛋白结合，但磁共振造影剂不与这些蛋白相互作用。静电力在X射线造影剂与人血清白蛋白形成复合物的过程中起重要作用。随着X射线造影剂分子尺寸的增加，它们对该蛋白结合位点的亲和力降低。X射线造影剂与人血浆γ-球蛋白形成复合物是通过疏水相互作用实现的。这些造影剂分子尺寸的增加会降低它们对γ-球蛋白结合位点的亲和力。
