| Literature DB >> 7603972 |
A Rescigno1, F Sollai, S Masala, M C Porcu, E Sanjust, A C Rinaldi, N Curreli, D Grifi, A Rinaldi.
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.Entities:
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Year: 1995 PMID： 7603972 DOI： 10.1080/10826069508010107
Source DB: PubMed Journal: Prep Biochem ISSN： 0032-7484