Dissociation kinetics of antigen-antibody interactions: studies on a panel of anti-albumin monoclonal antibodies.
Dissociation kinetics of antigen-antibody interactions: studies on a panel of anti-albumin monoclonal antibodies.
复制标题
抗原-抗体相互作用的解离动力学：对一组抗白蛋白单克隆抗体的研究。
DOI：
10.1016/0161-5890(89)90094-1
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发表时间：
1989
影响因子：
3.6
通讯作者：
Yarmush,ML
中科院分区：
文献类型：
--
作者：
Olson,WC;Spitznagel,TM;Yarmush,ML
本文报道了一组固定在琼脂糖微粒上的抗牛血清白蛋白单克隆抗体的动力学参数和平衡缔合常数。对于12个中等亲和力的共价固定化单克隆抗体（K= 0.25 × 108 - 1.2 × 108 M-1），测得的解离时间常数变化了两个数量级，从2.1到410分钟。直接测量的结合速率参数与从测量的平衡和解离速率参数计算的值一致。解离时间常数和平衡缔合常数也确定了8个单克隆抗体固定的生物特异性（通过他们的Fcregions）。一个显着降低K被观察到与这些单克隆抗体共价固定，而不是生物特异性固定。K值的降低反映了结合率的降低而不是解离率的增加。数据表明，对于本文所述的MAb，解离速率与平衡缔合常数不相关。
Kinetic parameters and equilibrium association constants (K) are reported for a panel of antibovine serum albumin (BSA) monoclonal antibodies (MAb) immobilized onto agarose particles. For 12 covalently immobilized MAb of moderate affinity (K= 0.25 × 108−1.2 × 108M−1) measured dissociation time constants varied two orders of magnitude, from 2.1 to 410 min. Directly measured association rate parameters agree with values calculated from measured equilibrium and dissociation rate parameters. Dissociation time constants and equilibrium association constants were also determined for eight MAb immobilized biospecifically (via their Fcregions). A significantly lowerKwas observed with those MAb which were covalently immobilized as opposed to biospecifically immobilized. These decreases inKappear to reflect decreased association rates rather than increased dissociation rates. The data suggest that, for the MAb described herein, dissociation rates do not correlate with equilibrium association constants.