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

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

  • Jutta Ludwig-Müller - , Johann Wolfgang Goethe-Universität Frankfurt am Main (Autor:in)
  • Thomas Rausch - , Johann Wolfgang Goethe-Universität Frankfurt am Main (Autor:in)
  • Siegfried Lang - , Johann Wolfgang Goethe-Universität Frankfurt am Main, Universität Heidelberg (Autor:in)
  • Willy Hilgenberg - , Johann Wolfgang Goethe-Universität Frankfurt am Main (Autor:in)

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

OriginalspracheEnglisch
Seiten (von - bis)1397-1400
Seitenumfang4
FachzeitschriftPhytochemistry
Jahrgang29
Ausgabenummer5
PublikationsstatusVeröffentlicht - 1990
Peer-Review-StatusJa
Extern publiziertJa

Schlagworte

Schlagwörter

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