Silberring J, Gołda W
Eur J Nucl Med. 1979 Dec;4(6):467-9. doi: 10.1007/BF00300848.
Insulin-125I antibody reaction was optimized by physical-chemical parameters. After the activation energies Ea and Ed for association and dissociation, respectively were calculated from the experimental data, the theoretical values of the reaction rate constants ka and kd were determined as well as equilibrium constants K. By means of the empirical formulae, the approximate incubation time for the RIA kit and maximal percent of insulin-125I binding to antibody (%B) in relation to temperature were computed. The proposed method may be applied to the new antigen-binder systems preparation (new antibodies, shortening of the incubation time, temperature changes, influence of different ions and kind of buffer).
通过物理化学参数优化胰岛素 - 125I抗体反应。从实验数据分别计算出结合和解离的活化能Ea和Ed后，确定反应速率常数ka和kd的理论值以及平衡常数K。借助经验公式，计算放射免疫分析试剂盒的近似孵育时间以及胰岛素 - 125I与抗体结合的最大百分比（%B）与温度的关系。所提出的方法可应用于新抗原 - 结合剂系统的制备（新抗体、缩短孵育时间、温度变化、不同离子的影响以及缓冲液种类）。
