Demonstration of an upper limit to the range of association rate constants amenable to study by biosensor technology based on surface plasmon resonance
Demonstration of an upper limit to the range of association rate constants amenable to study by biosensor technology based on surface plasmon resonance
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DOI：
10.1006/abio.1996.0109
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发表时间：
1996-03-15
影响因子：
2.9
通讯作者：
Winzor, DJ
中科院分区：
文献类型：
--
作者：
Hall, DR;Cann, JR;Winzor, DJ
BIAcore 传感图的数值模拟强调需要关注当前大分子相互作用速率常数测定中固有的假设，即流动相中溶质的浓度在其注入值下保持恒定。该假设对于有效关联速率常数等于或小于 10(5) M(-1) s(-1)（抗体与蛋白质抗原相互作用的特征值）的系统有效。然而，当有效关联速率常数提高到 10(7) M(-1) s(-1) 时，该假设失去有效性。后一个预测的基本正确性通过大豆胰蛋白酶抑制剂和固定化β-胰蛋白酶之间相互作用的实验研究得到了验证，固定化β-胰蛋白酶是一个具有可比反应动力学的系统。 (C) 1996 学术出版社
Numerical simulation of BIAcore sensorgrams has highlighted the need for concern about an assumption, inherent in current determinations of rate constants for macromolecular interactions, that the concentration of solute in the flowing phase remains constant at its injected value. This assumption is shown to be valid for systems with effective association rate constants equal to or less than 10(5) M(-1) s(-1), values characteristic of antibody interactions with protein antigens, However, the assumption loses validity when the effective association rate constant is raised to 10(7) M(-1) s(-1). The basic correctness of the latter prediction is verified by an experimental study of the interaction between soybean trypsin inhibitor and immobilized beta-trypsin, a system with comparable reaction kinetics. (C) 1996 Academic Press, Inc.