STUDIES ON ARACHIDONATE 5-LIPOXYGENASE OF RAT BASOPHILIC LEUKEMIA-CELLS

  • 1 January 1984
    • journal article
    • research article
    • Vol. 795  (3) , 458-465
Abstract
Arachidonate 5-lipoxygenase was partially purified from rat basophilic leukemia cells with the aid of ATP as a ligand linked to Sepharose. The enzyme produced predominantly 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid. Ca was required for the enzyme activity (0.1 mM for half maximal activity), and the C-dependent reaction was stimulated by ATP and several nucleotides. 5,8,11,14,17-Eicosapentaenoic acid was converted to its 5-hydroperoxy derivative at a higher rate than arachidonate oxygenation. 5,8,11-Eicosatrienoic acid as substrate was almost as active as arachidonic acid. Among various lipoxygenase inhibitors tested, cirsiliol, a flavone derivative, was the most potent.

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