Arachidonate 15-lipoxygenase from human eosinophil-enriched leukocytes: partial purification and properties

Biochem Biophys Res Commun. 1988 Jan 15;150(1):376-83. doi: 10.1016/0006-291x(88)90531-1.


Arachidonate 15-lipoxygenase was purified from human eosinophil-enriched leukocytes after showing that 15-lipoxygenase activity was 100-fold greater in eosinophils than in neutrophils. Partial purification was achieved using ammonium sulfate precipitation, cation-exchange and hydrophobic-interaction chromatography. New evidence is presented suggesting that 15-lipoxygenase has electrostatic and hydrophobic properties distinct from 5-lipoxygenase. In addition, ATP is shown to inhibit, and phosphatidylcholine is shown to stimulate, 15-lipoxygenase, suggesting a regulatory role for these compounds in the lipoxygenation of arachidonic acid.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / pharmacology
  • Arachidonate 15-Lipoxygenase / blood*
  • Arachidonate 5-Lipoxygenase / blood
  • Arachidonate Lipoxygenases / blood*
  • Chromatography
  • Chromatography, Ion Exchange
  • Eosinophils / enzymology*
  • Fractional Precipitation
  • Humans
  • Hydrogen-Ion Concentration
  • Hydroxyeicosatetraenoic Acids / blood
  • Leukocytes / enzymology*
  • Lipoxygenase Inhibitors
  • Neutrophils / enzymology
  • Phosphatidylcholines / pharmacology


  • Hydroxyeicosatetraenoic Acids
  • Lipoxygenase Inhibitors
  • Phosphatidylcholines
  • 15-hydroxy-5,8,11,13-eicosatetraenoic acid
  • Adenosine Triphosphate
  • Arachidonate Lipoxygenases
  • Arachidonate 15-Lipoxygenase
  • Arachidonate 5-Lipoxygenase