The subcellular localization of NAD- and NADP-linked glutamate dehydrogenases (GDH-NAD and GDH-NADP), alanine aminotransferase (ALAT) and aspartate aminotransferase (ASAT) in epimastigotes of Trypanosoma cruzi was studied by digitonin extraction from whole cells, subcellular fractionation by differential centrifugation. A and isopycnic ultracentrifugation. All enzymes presented both a cytosolic and a mitochondrial form; in addition, GDH-NADP seems to have a third, still undefined, localization. The results are compatible with the existence of two pathways for the production of L-alanine linked to the reoxidation of glycolytic NADH, one operative in the mitochondrion and the other in the cytosol, and perhaps responsible for the existence of the two alanine pools detected by 13C-nuclear magnetic resonance (B. Frydman et al., Eur. J. Biocbem. 192 (1990) 363-368). © 1991.
Documento: | Artículo |
Título: | Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
Autor: | Duschak, V.G.; Cazzulo, J.J. |
Filiación: | Instituto de Investigaciones Bioquímicas 'Luis F. Leloir', Fundación Campomar - CONICET - Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina |
Palabras clave: | Alanine aminotransferase; Glutamate dehydrogenase; Trypanosoma cruzi; alanine aminotransferase; glutamate dehydrogenase; nicotinamide adenine dinucleotide; nicotinamide adenine dinucleotide phosphate; alanine aminotransferase; aspartate aminotransferase; glutamate dehydrogenase; animal cell; animal tissue; article; cell fractionation; enzyme localization; mitochondrion; nonhuman; nuclear magnetic resonance; priority journal; trypanosoma cruzi; animal; biological model; density gradient centrifugation; enzymology; glycolysis; kinetics; metabolism; physiology; Trypanosoma cruzi; Animalia; Trypanosoma; Trypanosoma cruzi; Alanine Transaminase; Animal; Aspartate Aminotransferases; Cell Fractionation; Centrifugation, Density Gradient; Glutamate Dehydrogenase; Glycolysis; Kinetics; Models, Biological; Subcellular Fractions; Support, Non-U.S. Gov't; Trypanosoma cruzi |
Año: | 1991 |
Volumen: | 83 |
Número: | 2 |
Página de inicio: | 131 |
Página de fin: | 135 |
Título revista: | FEMS Microbiology Letters |
Título revista abreviado: | FEMS Microbiol. Lett. |
ISSN: | 03781097 |
CODEN: | FMLED |
CAS: | Alanine Transaminase, EC 2.6.1.2; Aspartate Aminotransferases, EC 2.6.1.1; Glutamate Dehydrogenase, EC 1.4.1.2 |
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v83_n2_p131_Duschak |