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

Research output: Contribution to journal › Research article › Contributed › peer-review

Contributors

  • Jutta Ludwig‐Müller - , Goethe University Frankfurt a.M. (Author)
  • Willy Hilgenberg - , Goethe University Frankfurt a.M. (Author)

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

Original languageEnglish
Pages (from-to)613-619
Number of pages7
JournalPhysiologia plantarum
Volume77
Issue number4
Publication statusPublished - Dec 1989
Peer-reviewedYes
Externally publishedYes

Keywords

ASJC Scopus subject areas

Keywords

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