PURIFICATION AND CHARACTERIZATION OF AN NAD(P)H-QUINONE OXIDOREDUCTASE FROM GLYCINE-MAX SEEDLINGS

Authors
RESCIGNO A SOLLAI F MASALA S PORCU MC SANJUST E RINALDI AC CURRELI N GRIFI D RINALDI A
Citation
A. Rescigno et al., PURIFICATION AND CHARACTERIZATION OF AN NAD(P)H-QUINONE OXIDOREDUCTASE FROM GLYCINE-MAX SEEDLINGS, Preparative biochemistry, 25(1-2), 1995, pp. 57-67
Citations number
16
Categorie Soggetti
Biology
Journal title
Preparative biochemistry → ACNP
ISSN journal
00327484
Volume
25
Issue
1-2
Year of publication
1995
Pages
57 - 67
Database
ISI
SICI code
0032-7484(1995)25:1-2<57:PACOAN>2.0.ZU;2-0
Abstract
An NAD(P)H:(quinone acceptor) oxidoreductase (EC 1.6.99.2) was purifie d from Glycine max seedlings by means of chromatographic procedures. A fter 1371-fold purification, the enzyme showed a single band in IEF co rresponding to an isoelectric point of 6.1. A single band was also fou nd in native-PAGE both by; activity staining and Coomassie brilliant b lue 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 oxid oreductase was able to use NADH or NADPH as the electron donor. Among the artificial quinones which are reduced by this enzyme, 6-hydroxydop a- and 6-hydroxydopamine-quinone are of particular interest because of their neurotoxic effects.