Natural polyamines inhibit soybean (Glycine max) lipoxygenase-1, but not the lipoxygenase-2 isozyme

Mauro MacCarrone, Argelinda Baroni, Alessandro Finazzi-Agrò

Research output: Contribution to journalArticlepeer-review


Natural polyamines are shown to inhibit dioxygenase activity of soybean lipoxygenase-1, but they were ineffective toward the lipoxygenase-2 isozyme. The inhibitory power was dependent on the number of basic groups in the molecule, in the order spermine > spermidine > cadaverine ≤ putrescine. Both spermidine and spermine acted as uncompetitive inhibitors of lipoxygenase-1 with respect to linoleic acid, the inhibition constants being 2.70 and 0.80 mM, respectively. The inhibitory power apparently correlated with the radical-trapping ability of the polyamines. Spermidine and spermine also inhibited the co-oxidase and peroxidase activities of lipoxygenase-1 and were effective inhibitors of lipoxygenase activity in lentil root protoplasts.

Original languageEnglish
Pages (from-to)35-40
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - Aug 1 1998


  • Oxodienes
  • Protoplasts
  • Radical-trapping ability

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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