Plasma membrane bound high pI peroxidase isoenzymes convert tryptophan to indole-3-acetaldoxime

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Jutta Ludwig-Müller - , Goethe University Frankfurt a.M. (Author)
  • Thomas Rausch - , Goethe University Frankfurt a.M. (Author)
  • Siegfried Lang - , Goethe University Frankfurt a.M., Heidelberg University  (Author)
  • Willy Hilgenberg - , Goethe University Frankfurt a.M. (Author)

Abstract

-Several peroxidase isoenzymes (pI 8-9) from phase-partitioned Chinese cabbage plasma membrane oxidized l-tryptophan to indole-3-acetaldoxime as shown by (i) correlation of catalytic activity with benzidineguaiacol staining on isoelectric focussing (IEF) gels, (ii) inhibition of enzyme activity by polyclonal antisera directed against tobacco peroxidase isoenzymes (which cross-react with Chinese cabbage peroxidases) and (iii) inhibition of tetraguaiacol formation by l-tryptophan. Treatment of the outside-out plasma membrane vesicles with 1 M sodium chloride and sonification released only part of the membrane-bound tryptophan oxidizing enzyme activity, suggesting little non-specific binding of peroxidases to (or trapping in) the membrane vesicles.

Details

Original languageEnglish
Pages (from-to)1397-1400
Number of pages4
JournalPhytochemistry
Volume29
Issue number5
Publication statusPublished - 1990
Peer-reviewedYes
Externally publishedYes

Keywords

Keywords

  • Brassica campestris subsp. pekinensis, Brassicaceae, Chinese cabbage, indole-3-acetaldoxime peroxidase isoenzymes, l-tryptophan.