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14-3-3 proteins intact with a 13-lipoxygenase, but not with a 9-lipoxygenase.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • Wessel L. Holtman
  • Michael R. Roberts
  • Berry J. Oppedijk
  • Christa Testerink
  • Mieke J. Van Zeijl
  • Mei Wang
<mark>Journal publication date</mark>26/05/2000
<mark>Journal</mark>FEBS Letters
Issue number1
Number of pages5
Pages (from-to)48-52
Publication StatusPublished
<mark>Original language</mark>English


Associations between lipoxygenases (Lox) and 14-3-3 proteins were demonstrated by two different methods. First, immunoprecipitation experiments, using isoenzyme-specific monoclonal Lox antibodies, showed that 14-3-3 proteins co-precipitate with 13-Lox, but not with the 9-Lox from barley. Second, interactions between 13-Lox and 14-3-3 were established by surface plasmon resonance studies, showing that 13-Lox binds with 14-3-3 proteins in a concentration-dependent manner. The interactions between 14-3-3 proteins and 13-Lox may reveal their role during plant development.