Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/40878
Share/Impact:
Título : Monoascorbate free radical-dependent oxidation-reduction reactions of liver Golgi apparatus membranes
Autor : Navas, Plácido, Sun, Iris, Crane, Frederick L., Morré, Dorothy M., Morré, D. James
Palabras clave : Golgi apparatus
Acidification
NADH ascorbate
β-NADP phosphorylase
Ascorbate free radical oxidoreductase
Rat liver
Dehydroascorbic acid
Oxidation-Reduction
Fecha de publicación : 14-Mar-2010
Editor: Springer
Resumen: Golgi apparatus from rat liver contain an ascorbate free radical oxidoreductase that oxidizes NADH at neutral pH with monodehydroascorbate as acceptor to generate a membrane potential. At pH 5.0, the reverse reaction occurs from NAD(+). The electron spin resonance signal of the ascorbate-free radical and its disappearance upon the addition of NADH (pH 7) or NAD(+) (pH 5.0) confirms monodehydroascorbate involvement. Location of monodehydroascorbate both external to and within Golgi apparatus compartments is suggested from energization provided by inward or outward flux of electrons across the Golgi apparatus membranes. The isolated membranes are sealed, oriented cytoplasmic side out and impermeable to NAD(+) and ascorbate. NAD(+) derived through the action of Golgi apparatus beta-NADP phosphohydrolase is simultaneously reduced to NADH with monodehydroascorbate present. The response of the NADH- (NAD(+)-) ascorbate free radical oxidoreductase system to pH in Golgi apparatus provides a simple regulatory mechanism to control vesicle acidification.
Descripción : 7 páginas, 6 figuras, 4 tablas.
Versión del editor: http://dx.doi.org/10.1007/s10863-010-9272-0
URI : http://hdl.handle.net/10261/40878
ISSN: 0145-479X
DOI: 10.1007/s10863-010-9272-0
Citación : Journal of Bioenergetics and Biomembranes 42(2): 181-187 (2010)
Referencias: PMID: 20229035
Appears in Collections:(CABD) Artículos

Files in This Item:
There are no files associated with this item.
Show full item record
 
CSIC SFX LinksSFX Query


Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.