Two distinct NAD(P)H-dependent redox enzymes isolated from onion root plasma membranes.
Plasma membranes purified by two-phase partition from onion roots catalyzed the NAD(P)H-dependent reduction of a variety of electron acceptor such as ferricyanide, quinones, dyes and ascorbate free radical. Among these, NAD(P)H-ferricyanide and -quinone oxidoreductase activities were effectively solubilized by Triton X-100. Both oxidoreductase activities were bound to an affinity column of Blue-Sepharose CL 6B. NADH eluted a redox enzyme showing more juglone than ferricyanide-dependent activity. Ulterior unspecific elution with salt allowed us to the partial purification of a different redox enzyme of about 31 kDa that reduced better ferricyanide than quinones and constituted the bulk of solubilized redox activity.
Serrano
A
A
Departamento de Biología Celular, Universidad de Córdoba, Spain.
Villalba
J M
JM
González-Reyes
J A
JA
Navas
P
P
Córdoba
F
F
D000490:Allium / Q000201:enzymology* / Q000648:ultrastructure; D002462:Cell Membrane / Q000201:enzymology; D003579:Cytochrome Reductases / Q000737:chemistry; D042966:Cytochrome-B(5) Reductase; D004579:Electron Transport; D008970:Molecular Weight; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry / Q000302:isolation & purification*; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification
D009247:NADH, NADPH Oxidoreductases; D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase; D016660:NAD(P)H Dehydrogenase (Quinone); C014227:ferricyanide reductase