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

RESCIGNO, ANTONIO;SANJUST, ENRICO;RINALDI, ANDREA;CURRELI, NICOLETTA;
1995-01-01

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.
1995
25
1-2
57
67
11
WOS:A1995QW28100005
2-s2.0-0029240385
http://www.tandfonline.com/doi/abs/10.1080/10826069508010107
Rescigno, Antonio; Sollai, F; Masala, S; Porcu, Mc; Sanjust, Enrico; Rinaldi, Andrea; Curreli, Nicoletta; Rinaldi, A.
1.1 Articolo in rivista
info:eu-repo/semantics/article
1 Contributo su Rivista::1.1 Articolo in rivista
262
8
none
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