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Titolo:
The membrane-bound L- and D-lactate dehydrogenase activities in mitochondria from Euglena gracilis
Autore:
Jasso-Chavez, R; Torres-Marquez, ME; Moreno-Sanchez, R;
Indirizzi:
Inst Nacl Cardiol, Dept Bioquim, Mexico City 14080, DF, Mexico Inst Nacl Cardiol Mexico City DF Mexico 14080 xico City 14080, DF, Mexico UNAM, Fac Med, Dept Bioquim, Mexico City 14080, DF, Mexico UNAM Mexico City DF Mexico 14080 t Bioquim, Mexico City 14080, DF, Mexico
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 2, volume: 390, anno: 2001,
pagine: 295 - 303
SICI:
0003-9861(20010615)390:2<295:TMLADD>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MITOCHONDRIA; ESCHERICHIA-COLI; MANDELATE DEHYDROGENASES; ACINETOBACTER-CALCOACETICUS; ELECTRON-TRANSPORT; PURIFICATION; BACTERIAL; FLAVOPROTEIN; EUKARYOTES; VESICLES;
Keywords:
respiratory chain; lactate dehydrogenase; stereo-specific enzymes; NAD(+)-independent dehydrogenation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Moreno-Sanchez, R Inst Nacl Cardiol, Dept Bioquim, Juan Badiano 1,Col Secc16, Mexico City 14080, DF, Mexico Inst Nacl Cardiol Juan Badiano 1,Col Secc 16 Mexico City DF Mexico 14080
Citazione:
R. Jasso-Chavez et al., "The membrane-bound L- and D-lactate dehydrogenase activities in mitochondria from Euglena gracilis", ARCH BIOCH, 390(2), 2001, pp. 295-303

Abstract

The activity of the pyridine nucleotide-independent lactate dehydrogenase (iLDH) was characterized in mitochondria isolated from the protist Euglena gracilis, The dissociation constants for L- and D-lactate were similar, butthe V-max was higher with the D isomer, A ping-pong kinetic mechanism was displayed with 2,4-dichlorophenol-indolphenol (DCPIP), or coenzyme Q(1), reacting as the second substrate with the modified, reduced enzyme. Oxamate was a competitive inhibitor against both L- and D-lactate, Oxalate exerted amixed type inhibition regarding L- or D-lactate and also against DCPIP, The rate of L-lactate uptake was partially inhibited by mersalyl and lower than the rate of dehydrogenation, which was mersalyl-insensitive, These data suggested that the active site of L-iLDH was orientated toward the intermembrane space. The following observations indicated the existence of two stereo-specific iLDH enzymes in the inner membrane of Euglena mitochondria: a greater affinity of the D-iLDH for both inhibitors, D-iLDH thermo-stability at 70 degreesC and denaturation of L-iLDH, opposite signs in the enthalpy change for the association reaction of the isomers to the enzyme, differential solubilization of both activities with detergents, and different molecular mass. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 06:47:07