Partial purification and characterization of PAF acetylhydrolase in human amniotic fluid

被引:2
|
作者
Son, SY
Kim, SH
Baek, SH
Chang, HW
机构
[1] YEUNGNAM UNIV,COLL PHARM,KYONGSAN 712749,SOUTH KOREA
[2] NISR,SEOUL,SOUTH KOREA
[3] EMORY UNIV,ATLANTA,GA 30322
关键词
PAF-acetylhydrolase; human amniotic fluid; oxidized phospholipid;
D O I
10.1007/BF02976148
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
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-PACE. In addition, the enzyme activity was inhibited by either diisopropylfluorophosphate(DFP) or p-bromophenacylbromide (pBPB), 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.
引用
收藏
页码:218 / 224
页数:7
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