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首页> 外文期刊>Artificial Organs >Plasma protein binding properties to immobilized heparin and heparin-albumin conjugate.
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Plasma protein binding properties to immobilized heparin and heparin-albumin conjugate.

机译：血浆蛋白与固定化肝素和肝素-白蛋白结合物的结合特性。

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Selective adhesion of plasma proteins to immobilized heparin is considered to be beneficial regarding hemocompatibility of foreign materials in contact with blood. Prothrombin, thrombin, antithrombin III (AT3), and fibrinogen were selected for analysis in an experimental model. Biomolecular interaction analysis employing surface plasmon resonance was utilized to record and analyze their binding properties in real time. Biotinylated heparin, heparin-albumin conjugate, and albumin, respectively, were immobilized onto streptavidin-coated sensors as ligands. Prothrombin did not bind to any of the ligand surfaces and no specific binding of any of the plasma proteins to albumin was observed. Binding kinetics of thrombin to heparin and to heparin-albumin conjugate were calculated using two different methods. For heparin, identical K(D)(equilibrium dissociation constant) values of 61 x 10(-9) M were obtained with both methods. For the conjugate, only slightly different K(D) values of 111 x 10(-9) and 104 x 10(-9) M, respectively, were calculated. The affinity of thrombin toward the heparin-coated surface proved to be higher than its affinity toward the heparin conjugate. The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process. Steady-state kinetic analysis revealed a K(D) value of 281 +/- 24 x 10(-9) M for the heparin surface. For the conjugate surface, a K(D) of 53 +/- 5 x 10(-9) M was calculated, indicating a higher affinity toward heparin-albumin conjugate. A high-affinity binding of fibrinogen to high-density surfaces of both heparin and the conjugate was observed. However, as binding to low-density surfaces was considerably reduced, specificity remained uncertain.
机译：对于异物与血液接触的血液相容性，血浆蛋白与固定化肝素的选择性粘附被认为是有益的。选择凝血酶原，凝血酶，抗凝血酶III（AT3）和纤维蛋白原在实验模型中进行分析。利用表面等离振子共振的生物分子相互作用分析被用来实时记录和分析它们的结合特性。生物素化的肝素，肝素-白蛋白结合物和白蛋白分别作为配体固定在链霉亲和素包被的传感器上。凝血酶原不结合任何配体表面，并且未观察到任何血浆蛋白与白蛋白的特异性结合。用两种不同方法计算凝血酶与肝素和肝素-白蛋白结合物的结合动力学。对于肝素，两种方法均获得相同的K（D）（平衡解离常数）值61 x 10（-9）M。对于缀合物，仅分别计算出分别略微不同的K（D）值111 x 10（-9）和104 x 10（-9）M。凝血酶对肝素涂层表面的亲和力被证明高于其对肝素结合物的亲和力。尽管是特异性的，AT3与肝素和肝素-白蛋白结合物的结合模式是双相的，可能是由于结合过程中的构象变化。稳态动力学分析表明，肝素表面的K（D）值为281 +/- 24 x 10（-9）M。对于缀合物表面，计算出的K（D）为53 +/- 5 x 10（-9）M，表明对肝素-白蛋白缀合物的亲和力更高。观察到纤维蛋白原与肝素和结合物的高密度表面的高亲和力结合。然而，由于与低密度表面的结合大大减少，特异性仍然不确定。

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