1921
Volume 40, Issue 2
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

The biologically active sulfidopeptide leukotriene, leukotriene C, is formed by the enzymatic action of leukotriene C synthase, which conjugates glutathione with leukotriene A. We have found that a filarial glutathione S-transferase can function as a leukotriene C synthase. Glutathione S-transferase was purified from the cytosol of adult by glutathione-agarose affinity chromatography and was reacted with 25 µM leukotriene A methyl ester and 10 mM glutathione. The filarial enzyme catalyzed the formation of leukotriene C methyl ester, as shown by reverse phase high pressure liquid chromatographic analyses. The finding that filarial glutathione S-transferase can function as a leukotriene C synthase provides a mechanism whereby filarial parasites could form lipoxygenase pathway derived sulfidopeptide leukotrienes.

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/content/journals/10.4269/ajtmh.1989.40.171
1989-02-01
2017-11-18
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