Son S Y, Kim S H, Baek S H, Chang H W
College of Pharmacy, Yeungnam University, 712-749, Gyongsan, Korea.
Arch Pharm Res. 1997 Jun;20(3):218-24. doi: 10.1007/BF02976148.
Platelet-activating factor (PAF) acetylhydrolase, which removes the acetyl moiety at thesn-2 position, has been found in human amniotic fluid. We purified this enzyme by ammonium sulfate precipitation, and sequential use of DEAE-Sepharose CL-6B, hydroxyapatite, chelating-Sepharose, and Mono Q column chromatographies. This enzyme exhibited broad pH optima and was unaffected by EDTA. Partially purified enzyme had a molecular weight of approximately 34 kDa on SDS-PAGE. In addition, the enzyme activity was inhibited by either diisopropylfluorophosphate(DFP) orp-bromophenacylbromide (p-BPB), suggesting that this enzyme possesses active serine and histidine residues. The enzyme showed similar activity towards PAF and oxidatively modified phosphatidylcholine, but didn't hydrolyze phosphatidylcholine or phosphatidylethanolamine with a long chain fatty acyl group atsn-2 position.
