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Monoclonal Antibody Binding to (Fluoro) Quinolones in Competitive Immunoassay: Quantitive Correlation Antibody Affinity with Molecular Parameters

机译:竞争性免疫测定中的(氟)喹诺酮类单克隆抗体结合:分子参数的定量相关抗体亲和力。

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@@ Antibodies used in competitive immunoassay tor the detection ot small molecule usually recognize one more molecules that share common epitopes with different affinities. For immunochemist, there is a challenging problem to well understand the cause of the antibody' s multi-specificity from only looking two-dimensional structural formulas of the compounds studied (Sanvicens et al.,2003). A method that can provide useful parameters about the topological and electrostatic properties of molecule can be sufficient in elucidating the diversity of antibody binding (Beier and Stanker 2001). In the study, we determinates the affinities of one monoclonal antibody (C4A9H1) to 14 (fluoro) quinolones by competitive ELISA and calculated molecular parameters of these (fluoro)quinolones by quantum chemical B3LYP/6-31G*.
机译:在竞争性免疫测定中用于检测小分子的抗体通常会识别另外一种分子,这些分子共享具有不同亲和力的共同表位。对于免疫化学家来说,仅从所研究化合物的二维结构式上看,就很难很好地理解抗体多特异性的原因(Sanvicens等,2003)。可以提供有关分子的拓扑和静电特性的有用参数的方法足以阐明抗体结合的多样性(Beier和Stanker 2001)。在这项研究中,我们通过竞争性ELISA确定了一种单克隆抗体(C4A9H1)与14种(氟)喹诺酮的亲和力,并通过量子化学B3LYP / 6-31G *计算了这些(氟)喹诺酮的分子参数。

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