Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi
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 differe...
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1991
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v83_n2_p131_Duschak http://hdl.handle.net/20.500.12110/paper_03781097_v83_n2_p131_Duschak |
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paper:paper_03781097_v83_n2_p131_Duschak2023-06-08T15:39:12Z Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi 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 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. 1991 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v83_n2_p131_Duschak http://hdl.handle.net/20.500.12110/paper_03781097_v83_n2_p131_Duschak |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| topic_facet |
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 |
| description |
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. |
| title |
Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| title_short |
Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| title_full |
Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| title_fullStr |
Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| title_full_unstemmed |
Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi |
| title_sort |
subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of trypanosoma cruzi |
| publishDate |
1991 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v83_n2_p131_Duschak http://hdl.handle.net/20.500.12110/paper_03781097_v83_n2_p131_Duschak |
| _version_ |
1768542507205918720 |