Nemerson Y
Department of Medicine, Mount Sinai School of Medicine, New York, NY 10029, USA.
Haemostasis. 1996 Oct;26 Suppl 4:98-101. doi: 10.1159/000217290.
In this paper we consider the assumptions that apply to the classical Michaelis-Menten enzyme kinetics and examine their applicability to a two-dimensional catalytic system. While we specifically address the kinetics of factor X activation catalyzed by a complex of tissue factor and factor VIIa, these concepts are applicable to any system in which both enzyme and substrate are membrane-bound. We emphasize the fact that the membranes become crowded with substrate and product molecules, thus rendering the assumption of "sparseness" inappropriate. Data from computer simulations are considered as well as preliminary laboratory experiments.
在本文中，我们考虑适用于经典米氏酶动力学的假设，并研究它们对二维催化系统的适用性。虽然我们具体探讨了组织因子与因子VIIa复合物催化因子X激活的动力学，但这些概念适用于酶和底物都结合在膜上的任何系统。我们强调这样一个事实，即膜上会挤满底物和产物分子，因此“稀疏性”假设并不适用。文中考虑了计算机模拟数据以及初步的实验室实验。
