Neri D, Montigiani S, Kirkham P M
Institute of Molecular Biology and Biophysics, ETH Hoenggerberg, Zürich, Switzerland.
Trends Biotechnol. 1996 Dec;14(12):465-70. doi: 10.1016/S0167-7799(96)10067-6.
Binding specificities against virtually any antigen can be isolated from antibody libraries displayed on filamentous phage. The determination of antibody-antigen affinity constants and binding kinetics is an important part of antibody characterization, and may be predictive of antibody performance in biotechnological applications. This article, intended as a guideline for the scientist who isolates a novel antibody and wishes to characterize its binding properties, presents the authors' view on widely used methodologies for the quantitative determination of antibody-antigen interactions.
针对几乎任何抗原的结合特异性都可以从展示在丝状噬菌体上的抗体文库中分离出来。抗体 - 抗原亲和力常数和结合动力学的测定是抗体表征的重要组成部分，并且可能预测抗体在生物技术应用中的性能。本文旨在为分离新型抗体并希望表征其结合特性的科学家提供指导方针，介绍了作者对广泛用于定量测定抗体 - 抗原相互作用的方法的看法。
