Purification of NADPH‐specific indole‐3‐acetaldehyde reductase from Cucumis sativus by two‐dimensional native polyacrylamide gel electrophoresis

Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung

Beitragende

  • Jutta Ludwig‐Müller - , Johann Wolfgang Goethe-Universität Frankfurt am Main (Autor:in)
  • Willy Hilgenberg - , Johann Wolfgang Goethe-Universität Frankfurt am Main (Autor:in)

Abstract

NADPH‐specific indole‐3‐acetaldehyde (IAAId) reductase from cucumber (Cucumis sativus L. <cv. Delikatess) was purified by several purification steps to one spot on a two‐dimensional polyacrylamide gel. The purification was 2000‐fold. IAAId reductase was shown to be a cytoplasmic enzyme by differential centrifugation and subsequent marker enzyme analysis. The substrates IAAId and dihydroxyacetone (DHA) do not seem to be converted by the same enzyme.

Details

OriginalspracheEnglisch
Seiten (von - bis)613-619
Seitenumfang7
FachzeitschriftPhysiologia plantarum
Jahrgang77
Ausgabenummer4
PublikationsstatusVeröffentlicht - Dez. 1989
Peer-Review-StatusJa
Extern publiziertJa

Schlagworte

ASJC Scopus Sachgebiete

Schlagwörter

  • Cucumber, Cucumis sativus, indole‐3‐acetaldehyde reductase, protein purification, two‐dimensional gel electrophoresis