Laboratoire d'Electrochimie Moléculaire, UMR 7591 CNRS, Université Paris Diderot, Sorbonne Paris Cité, 15 rue Jean-Antoine de Baïf, F-75205 Paris Cedex 13, France.
Langmuir. 2012 Oct 16;28(41):14665-71. doi: 10.1021/la3030827. Epub 2012 Oct 1.
In the present work, exact kinetic equations describing the action of an enzyme in solution on a substrate attached to a surface have been derived in the framework of the Michaelis-Menten mechanism but without resorting to the often-used steady-state approximation. The here-derived kinetic equations are cast in a workable format, allowing us to introduce a simple and universal procedure for the quantitative analysis of enzyme surface kinetics that is valid for any kinetic situation. The results presented here should allow experimentalists studying the kinetics of enzyme action on immobilized substrates to analyze their data in a perfectly rigorous way.
在目前的工作中，我们在 Michaelis-Menten 机制的框架内推导出了一个精确的描述酶在溶液中对附着在表面上的底物的作用的动力学方程，而没有使用经常使用的稳态近似。这里推导出的动力学方程采用了一种可行的格式，使我们能够引入一种简单而通用的方法，用于对任何动力学情况的酶表面动力学进行定量分析。这里呈现的结果应该使研究固定化底物上酶作用动力学的实验人员能够以一种完全严格的方式分析他们的数据。
