Purification of Human Serum Paraoxonase and Effect of Acetylsalicylic Acid on Paraoxonase Activity

摘要

Paraoxonase was purified from human serum using sepharose-4B-L-tyrosine-l-napthylamine affinity chro-matography. This enzyme was purified 1797-fold. SDS-polyacrylamide electrophoresis of the enzyme indicates a single protein staining band with an apparent Mr of 43 kDa. The kinetic properties of the purified enzyme were determined. The V_max and K_m are 231.5 ?/mg protein (EU) and 3.96 mM using substrate paraoxon respectively. The effect of acetylsalicylic acid on purified human serum paraoxonase has been investigated in vitro. The inhibition and activation effects of acetylsalicylic acid on serum paraoxonase activity were measured spectrophotometrically using paraoxon as the substrate.# #1 Dollars 1001N200308164Dollars 1200