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  • Title: Iodination of arachidonic acid mediated by eosinophil peroxidase, myeloperoxidase and lactoperoxidase. Identification and comparison of products.
    Author: Turk J, Henderson WR, Klebanoff SJ, Hubbard WC.
    Journal: Biochim Biophys Acta; 1983 Apr 13; 751(2):189-200. PubMed ID: 6299368.
    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.
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