Garrido-del Solo C, García-Cánovas F, Havsteen B H, Varón-Castellanos R
Departamento de Química-Física, Escuela Universitaria Politécnica, Universidad de Castilla-La Mancha, Albacete, Spain.
Biochem J. 1993 Sep 1;294 ( Pt 2)(Pt 2):459-64. doi: 10.1042/bj2940459.
A kinetic analysis of the Michaelis-Menten mechanism is made for the cases in which the free enzyme, or the enzyme-substrate complex, or both, are unstable, either spontaneously or as a result of the addition of a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentration. The validity of these equations has been checked by using numerical simulations. An experimental design and a kinetic data analysis allowing the evaluation of the parameters and kinetic constants are recommended.
针对游离酶、酶-底物复合物或两者自发地或因添加试剂而不稳定的情况,对米氏机制进行了动力学分析。在酶浓度受限的条件下,推导了所有相关物种的明确时间进程方程。通过数值模拟检验了这些方程的有效性。推荐了一种允许评估参数和动力学常数的实验设计和动力学数据分析方法。