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  • Title: Purification of lipoxygenase and hydroperoxide dehydrase in flaxseeds: interaction between these enzymatic activities.
    Author: Rabinovitch-Chable H, Cook-Moreau J, Breton JC, Rigaud M.
    Journal: Biochem Biophys Res Commun; 1992 Oct 30; 188(2):858-64. PubMed ID: 1359887.
    Abstract:
    We have purified two enzymic activities from flaxseed acetone powder: a lipoxygenase and a hydroperoxide dehydrase. The lipoxygenase activity belongs to an iron-containing protein having a molecular weight of 130 kDa which, upon incubation with alpha-linolenic acid, forms 13-hydroperoxy-9(Z), 11(E), 15(Z)- octadecatrienoic acid. The hydroperoxide dehydrase (a 55 kDa protein) metabolizes this hydroperoxide to an allene oxide which in turn is spontaneously hydrolyzed to alpha- and gamma-ketols. Relationships between these two enzymes were studied and results suggest an inhibition of the lipoxygenase by hydroperoxide dehydrase.
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