Serum paraoxonase 1 (PON1) was purified from bovine serum using hydrophobic interaction chromotography on Sepharose 4B-coupled l-tyrosine 1-naphthylamine gel, and monitored by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Paraoxonase enzyme was immobilized using different ratios of glutaraldehyde and the maximum activity was observed with 7% glutaraldehyde. The effects of inhibition by Mn(+2), Co(+2) and Cu(+2) heavy metals on the immobilized and free enzyme activities were studied. At the optimum pH and temperature, the K(m) and V(max) kinetic values for bovine serum paraoxonase and immobilized paraoxonase towards paraoxon substrate were determined as 0.296 × 10(-3) M & 37.04 EU vs. 0.727-10(-3) M & 36.36 EU, respectively.
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