Nitrate reductase from Spinacea oleracea. FAD and the reactivation of the enzyme treated with p-Hydroxymercuribenzoate

F. Castillo
F.F. de la Rosa
E. Palacián
58

Abstract

Spinach nitrate reductase complex previously inactivated by treatment with mercurials p-hydroxymercuribenzoate or p-hydroxymercuriphenyl sulphonate can be reactivated by incubation with dithioerythritol. The reactivation of NADH-diaphorase seems to be FAD-dependent, whereas that of FNH2-nitrate reductase is not. The requirement of FAD for NADH-inactivation of nitrate reductase treated with p-hydroxymercuribenzoate disappears after treatment with dithioerythritol.

Keywords:
Dihydrolipoamide Dehydrogenase/analysis, Enzyme Reactivators, Flavin-Adenine Dinucleotide/analysis, Mercuribenzoates/pharmacology, Nitrate Reductases/analysis, Vegetables/analysis

Authors

F. Castillo
F.F. de la Rosa
E. Palacián


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