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

RESCIGNO, ANTONIO;SOLLAI F;MASALA S;PORCU MC;SANJUST, ENRICO;RINALDI, ANDREA;CURRELI, NICOLETTA;RINALDI A.

1995-01-01

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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.