NADH-specific dehydrogenase from onion root plasma membrane: purification and characterization |
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Authors: | A. Serrano F. Córdoba J. A. González-Reyes C. Santos P. Navas J. M. Villalba |
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Affiliation: | (1) Departamento de Biología Celular, Facultad de Ciencias, Universidad de Cordoba, Avda. San Alberto Magno s/n, E-14004 Córdoba, Spain;(2) Present address: Departamento de Ciencias Agroforestales, Universidad de Huelva, Huelva, Spain |
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Abstract: | Summary Plasma membranes isolated from onion roots by twophase partition contain at least two different NAD(P)H-dehydrogenases. A 27 kDa electron transport protein oxidises both NADH and NADPH and exhibits maximal activity with quinones as electron acceptors. A distinct 31 kDa dehydrogenase is specific for NADH as donor and shows maximal activity with ferricyanide. This novel enzyme is responsible for most NADH-ferricyanide oxidoreductase activity of solubilized onion root plasma membranes and exhibits properties different to other purified NAD(P)H-dehydrogenases.Abbreviations DES diethylstilbestrol - FeCN potassium ferricyanide - NBT nitroblue tetrazolium - PHMB p-hydroxymercuribenzoate - PMSF phenylmethylsulfonylfluoride - PTA phosphotungstic acid - SHAM salicylhydroxamic acid - TTFA thenoyltrifluoroacetone |
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Keywords: | NADH-dehydrogenase Onion root Plasma membrane Protein purification Redox system |
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