Iodination of arachidonic acid mediated by eosinophil peroxidase, myeloperoxidase and lactoperoxidase identification and comparison of products

John Turk, William R. Henderson, Seymour J. Klebanoff, Walter C. Hubbard

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Arachidonic acid undergoes iodination in the presence of hydrogen peroxide, iodide, and either eosinophil peroxidase, myeloperoxidase or lactoperoxidase. The profile of products generated by each of the three peroxidases is similar as determined by reversed-phase high-performance liquid chromatography. Structural analysis of the products indicate that: 1, each of the four double bonds in arachidonic acid is susceptible to iodination; 2, arachidonic acid can be multiply iodinated; and 3, the carboxylate moiety does not participate in the formation of all products. The isomeric composition of the isolated products indicates that peroxidase-mediated iodination of arachidonate is not stereoselective.

Original languageEnglish
Pages (from-to)189-200
Number of pages12
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume751
Issue number2
DOIs
StatePublished - Apr 13 1983
Externally publishedYes

Keywords

  • Arachidonic acid
  • Iodination
  • Lactoperoxidase
  • Myeloperoxidase
  • Peroxidase

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