Patel Samir P, Katyare Surendra S
Department of Biochemistry, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara, Gujarat, India.
Z Naturforsch C J Biosci. 2005 Sep-Oct;60(9-10):785-91. doi: 10.1515/znc-2005-9-1020.
Substrate kinetic properties of cytochrome oxidase in rat liver, kidney, brain and heart mitochondria were examined using ascorbate + N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD) as the electron donor system. Analysis of the substrate kinetics data revealed tissue-specific expression of kinetic components exhibiting differences with respect to Km, Vmax and Kcat/Km values. Regression analysis data suggest that the enzyme activity may be regulated in a tissue-specific manner.
使用抗坏血酸 + N,N,N',N'-四甲基对苯二胺(TMPD)作为电子供体系统,检测了大鼠肝脏、肾脏、大脑和心脏线粒体中细胞色素氧化酶的底物动力学特性。对底物动力学数据的分析揭示了动力学组分的组织特异性表达,在米氏常数(Km)、最大反应速度(Vmax)和催化常数与米氏常数的比值(Kcat/Km)值方面存在差异。回归分析数据表明,该酶活性可能以组织特异性方式受到调节。