Rakitzis E T
Department of Biological Chemistry, University of Athens Medical School, Greece.
Biochem J. 1989 Nov 1;263(3):855-9. doi: 10.1042/bj2630855.
A kinetic analysis is presented of reactions of protein modification, and/or of modification-induced enzyme inactivation, which can formally be described by a single exponential function, or by a summation of two exponential functions, of reaction time plus a constant term. The reaction schemes compatible with the kinetic formalism of these cases are given, and a simple kinetic criterion is described whereby the identification of one of these cases, strong negative protein modification co-operativity, may be carried out. The treatment outlined in this paper is applied to a case from the literature, the inactivation of glyceraldehyde-3-phosphate dehydrogenase by butane-2,3-dione [Asriyants, Benkevich & Nagradova (1983) Biokhimiya (Engl. Transl.) 48, 164-171].
本文对蛋白质修饰反应和/或修饰诱导的酶失活反应进行了动力学分析,这些反应形式上可以用反应时间的单指数函数或两个指数函数之和加上一个常数项来描述。给出了与这些情况的动力学形式相符的反应方案,并描述了一个简单的动力学标准,据此可以识别其中一种情况,即强负性蛋白质修饰协同性。本文概述的处理方法应用于文献中的一个案例,即丁二酮对3-磷酸甘油醛脱氢酶的失活作用[阿斯里扬茨、本科维奇和纳格拉多娃(1983年)《生物化学》(英文译本)48, 164 - 171]。