Purification of lipoxygenase and hydroperoxide dehydrase in flaxseeds: Interaction between these enzymatic activities

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 α-linolenic acid, forms 13-hydroperoxy-9(Z), 11 (E), 1...

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Veröffentlicht in:Biochemical and biophysical research communications 1992-10, Vol.188 (2), p.858-864
Hauptverfasser: Rabinovitch-Chable, Hélène, Cook-Moreau, Jeanne, Breton, Jean-Christian, Rigaud, Michel
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Sprache:eng
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Zusammenfassung: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 α-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 α-and γ-ketols. Relationships between these two enzymes were studied and results suggest an inhibition of the lipoxygenase by hydroperoxide dehydrase.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(92)91135-D