Literature DB >> 6679313

NADH-monodehydroascorbate reductase in human erythrocyte membranes.

H Goldenberg, C Grebing, H Löw.   

Abstract

Enzymatic activity of NADH-monodehydroascorbate reductase could be observed in red blood cell membranes. This activity was latent in right side out as well as inside out vesicles. Apart from this latency addition of certain detergents led to activation of the enzyme also in open membrane preparations. The enzyme was inhibited by metal chelators, and displayed a very low apparent Michaelis constant. Monodehydroascorbate is a candidate for the natural electron acceptor of the transmembrane NADH-oxido-reductase. The activation by detergent may be due to enhancement of lipid fluidity or to exposure of a lipophilic substrate binding site.

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Year:  1983        PMID： 6679313

Source DB:  PubMed          Journal:  Biochem Int        ISSN： 0158-5231


  9 in total

1.  The ascorbate: ascorbate free radical oxidoreductase from the erythrocyte membrane is not cytochrome b561.

Authors:  M M Van Duijn; J T Buijs; J Van der Zee; P J Van den Broek
Journal:  Protoplasma       Date:  2001       Impact factor: 3.356

2.  Peroxisomal monodehydroascorbate reductase. Genomic clone characterization and functional analysis under environmental stress conditions.

Authors:  Marina Leterrier; Francisco J Corpas; Juan B Barroso; Luisa M Sandalio; Luis A del Río
Journal:  Plant Physiol       Date:  2005-07-29       Impact factor: 8.340

Review 3.  Electron and proton transport across the plasma membrane.

Authors:  F L Crane; I L Sun; R Barr; H Löw
Journal:  J Bioenerg Biomembr       Date:  1991-10       Impact factor: 2.945

4.  NADH-ascorbate free radical and -ferricyanide reductase activities represent different levels of plasma membrane electron transport.

Authors:  J M Villalba; A Canalejo; J C Rodríguez-Aguilera; M I Burón; D J Mooré; P Navas
Journal:  J Bioenerg Biomembr       Date:  1993-08       Impact factor: 2.945

5.  Monoascorbate free radical-dependent oxidation-reduction reactions of liver Golgi apparatus membranes.

Authors:  Placido Navas; Iris Sun; Frederick L Crane; Dorothy M Morré; D James Morré
Journal:  J Bioenerg Biomembr       Date:  2010-03-13       Impact factor: 2.945

6.  Interactions between ascorbyl free radical and coenzyme Q at the plasma membrane.

Authors:  A Arroyo; F Navarro; C Gómez-Díaz; F L Crane; F J Alcaín; P Navas; J M Villalba
Journal:  J Bioenerg Biomembr       Date:  2000-04       Impact factor: 2.945

7.  Assessing the reductive capacity of cells by measuring the recycling of ascorbic and lipoic acids.

Authors:  James M May
Journal:  Methods Mol Biol       Date:  2010

Review 8.  Extracellular ascorbate stabilization: enzymatic or chemical process?

Authors:  J C Rodríguez-Aguilera; P Navas
Journal:  J Bioenerg Biomembr       Date:  1994-08       Impact factor: 2.945

9.  Iron-induced ascorbate oxidation in plasma as monitored by ascorbate free radical formation. No spin-trapping evidence for the hydroxyl radical in iron-overloaded plasma.

Authors:  M Minetti; T Forte; M Soriani; V Quaresima; A Menditto; M Ferrari
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857
  9 in total

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