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KMID : 0043319970200030218
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Archives of Pharmacal Research
1997 Volume.20 No. 3 p.218 ~ p.224
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Partial Purification and Characterization of PAF Acetylhydrolase in Human Amniotic Fluid
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Son So-Young
Kim So-Hee
Baek Suk-Hwan
Chang Hyun-Wook
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Abstract
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Platelet-activating factor (PAF) acetylhydrolase, which removes the acetyl moiety at the sn-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) or p-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 at sn-2 position.
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KEYWORD
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PAF-acetylhydrolase, Human amniotic fluid, Oxidized phospholipid
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