Purification and characterization of an NAD(P)H:quinone oxidoreductase from Glycine max seedlings

Prep Biochem. 1995 Feb-May;25(1-2):57-67. doi: 10.1080/10826069508010107.

Abstract

An NAD(P)H:(quinone acceptor) oxidoreductase (EC 1.6.99.2) was purified from Glycine max seedlings by means of chromatographic procedures. After 1371-fold purification, the enzyme showed a single band in IEF corresponding to an isoelectric point of 6.1. A single band was also found in native-PAGE both by activity staining and Coomassie brilliant blue staining. The molecular mass determined in SDS-PAGE was 21900 Da, while in HPLC gel-filtration it was 61000 Da. The NAD(P)H:quinone oxidoreductase was able to use NADH or NADPH as the electron donor. Among the artificial quinones which are reduced by this enzyme, 6-hydroxydopa- and 6-hydroxydopamine-quinone are of particular interest because of their neurotoxic effects.

MeSH terms

  • 2,6-Dichloroindophenol / metabolism
  • Electron Transport
  • Electrophoresis, Polyacrylamide Gel
  • Glycine max / enzymology*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • NAD / metabolism
  • NAD(P)H Dehydrogenase (Quinone) / antagonists & inhibitors
  • NAD(P)H Dehydrogenase (Quinone) / chemistry
  • NAD(P)H Dehydrogenase (Quinone) / isolation & purification*
  • NAD(P)H Dehydrogenase (Quinone) / metabolism
  • NADP / metabolism
  • Plants / enzymology
  • Spectrophotometry
  • Substrate Specificity
  • Temperature

Substances

  • NAD
  • NADP
  • 2,6-Dichloroindophenol
  • NAD(P)H Dehydrogenase (Quinone)