Le Saux T, Varenne A, Perreau F, Siret L, Duteil S, Duhau L, Gareil P
Laboratoire d'Electrochimie et Chimie Analytique, UMR CNRS 7575, Ecole Nationale Supérieure de Chimie de Paris, Université ParisVI, 11, rue Pierre et Marie Curie, 75231 Paris Cedex 05, France.
J Chromatogr A. 2006 Nov 3;1132(1-2):289-96. doi: 10.1016/j.chroma.2006.07.092. Epub 2006 Sep 11.
The suitability of affinity capillary electrophoresis (ACE) and frontal analysis continuous capillary electrophoresis (FACCE) for binding constant determination was investigated for complexes between heparin fragments and antithrombin III, one of the main target proteins in the coagulation cascade. In a 100 mM ionic strength phosphate buffer (pH 7.4), ACE was suitable to determine weak to medium interactions developed by short oligomeric heparin fragments, but it failed for decasaccharide, which presents a more complex irreversible interaction. However FACCE allowed evaluating the binding constant for these longer oligomeric fragments. Both experimental approaches were complementary for a wide variety of heparinic fragments.
研究了亲和毛细管电泳（ACE）和前沿分析连续毛细管电泳（FACCE）在测定凝血级联反应中主要靶蛋白之一抗凝血酶III与肝素片段形成的复合物结合常数方面的适用性。在100 mM离子强度的磷酸盐缓冲液（pH 7.4）中，ACE适用于测定短寡聚肝素片段形成的弱至中等强度的相互作用，但对于十糖则不适用，因为十糖存在更复杂的不可逆相互作用。然而，FACCE能够评估这些较长寡聚片段的结合常数。这两种实验方法对于多种肝素片段具有互补性。
