steady-state kinetics of roystonea regia palm tree peroxidase稳态动力学roystonea regia棕榈树过氧化物酶.pdf

Vol.3, No.1, 16-28 (2012) Journal of Biophysical Chemistry /10.4236/jbpc.2012.31002 Steady-state kinetics of Roystonea regia palm tree peroxidase 1 1 1 Laura Sánchez Zamorano , Nazaret Hidalgo Cuadrado , Patricia Pérez Galende , Manuel G. Roig1*, Valery L. Shnyrov2 1Departamento de Química Física, Facultad de Química, Universidad de Salamanca, Salamanca, Spain; * Corresponding Author: mgr@usal.es 2Departamento de Bioquímica y Biología Molecular, Facultad de Biología, Universidad de Salamanca, Salamanca, Spain Received 12 October 2011; revised 20 November 2011; accepted 5 December 2011 ABSTRACT Peroxide Royal palm tree peroxidase (RPTP) has been isolated to homogeneity from leaves of Roys- 1. INTRODUCTION tonea regia palm trees. The enzyme purification Peroxidases (EC ; donor: hydrogen peroxide steps included homogenization, (NH4)SO4 pre- oxidoreductase) are widely distributed in the living world cipitation, extraction of palm leaf colored com- and are involved in many physiological processes. The pounds and consecutive chromatography on Ph- oxidation of many biological substances in body fluids enyl-Sepharose, TSK-Gel DEAE-5PW and Super- leads to the production of a certain amount of hydrogen dex-200. The novel peroxidase