Perez-Gilabert M, Sanchez-Ferrer A, Garcia-Carmona F
Departamento de Bioquímica, Facultad de Biología, Universidad de Murcia, Spain.
Biochem J. 1992 Dec 15;288 ( Pt 3)(Pt 3):1011-5. doi: 10.1042/bj2881011.
A new plot for explaining the complex expression of the enzymic activity in reverse micelles has been developed as an extension of the theoretical model described by our group [Bru, Sánchez-Ferrer & García-Carmona (1990) Biochem. J. 268, 679-684]. The plot describes the changes in the relative volume, amount of enzyme (mumoles), enzyme concentration (microM) and substrate concentration (microM) in the phase where the enzyme is active. To illustrate the usefulness of this plot, the complex activity of soya bean lipoxygenase in reverse micelles acting on its interfacial substrate, octadecadienoic acid, was studied. It showed the key parameters ruling the activity profiles of lipoxygenase with respect to micelle size (omega 0), micelle concentration (theta) and the substrate/surfactant molar ratio (rho), which have never been described before.
作为我们团队所描述理论模型[布鲁、桑切斯 - 费雷尔和加西亚 - 卡尔莫纳(1990年)《生物化学杂志》268卷,679 - 684页]的扩展,已开发出一种新的图表来解释反胶束中酶活性的复杂表达。该图表描述了酶具有活性的相中相对体积、酶量(微摩尔)、酶浓度(微摩尔)和底物浓度(微摩尔)的变化。为说明此图表的实用性,研究了大豆脂氧合酶在反胶束中作用于其界面底物十八碳二烯酸时的复杂活性。它展示了决定脂氧合酶活性曲线的关键参数,这些参数与胶束大小(ω0)、胶束浓度(θ)和底物/表面活性剂摩尔比(ρ)有关,而这些参数此前从未被描述过。