Abstract

ISOLATION AND STUDYING ENZYME PARAOXOASE FORM NORMAL HUMAN PLASMA

Prof. Tareq Y. Ahmed and *Lana Abid Mansor

ABSTRACT

The research was concerned with isolation and characterization of paraoxonase from normal human plasma using different biochemical techniques. Which included: ammonium sulfate precipitation, dialysis, lon exchanger chromatography on DEAE – cellulose sephadex G50 fast flow and gel filtration on sephadex G75. The apparent molecular weight of the isolated paraoxnase(PON1) using gel fittration chromatography and SDS electrophoresis was determined and found to be (42000) Dalton. Finally, there search specifies the optimum condition from paraoxonase activity. Maximum activity was obtained using (7Mm) of paraoxon as substrate for the enzyme, Tris- HCl (70 mM) as a buffer at PH (8) for (25) minutes at(45)c° using lineweaver – burk plot it was found that maximum velocity (v max) and michaelis-Menien constant (km) had the values of (5μmol/min) and (3.335) mM respectively. This work is taken from her ph. thesis.

Keywords: paraoxonase, fittration, lineweaver – burk, michaelis-Menien, respectively.