Novel purification strategy for paraoxonase enzyme

Abstract

Human serum paraoxonase (PON1, EC 3.1.8.1.) is a high-den-sity lipid (HDL)-associated, calcium-dependent enzyme; its physi-ological substrates are not known. Paraoxonase bound to HDLis an important liver enzyme responsible for prevention of lipidperoxide accumulation in low-density lipoprotein (LDL), bacte-rial endotoxins and hydrolyses OP insecticides and nerve gases.In this study, a new purification strategy for human PON1enzyme will develop using two-step procedures, namely ammo-nium sulfate precipitation and sepharose-4B-l-tyrosine-3-amin-ophenantrene hydrophobic interaction chromatography. Overallpurification rate of our method will found. The V(max) andK(m) of the purified enzyme will determined.