Presence and subcellular localization of tyrosine aminotransferase and p-hydroxyphenyllactate dehydrogenase in epimastigotes of Trypanosoma cruzi

Cell-free extracts of epimastigotes of Trypanosoma cruzi contain tyrosine aminotransferase (TAT) and p-hydroxyphenyllactate dehydrogenase (pHPLDH). The TAT activity could be separated from aspartate aminotransferase (ASAT) by polyacrylamide gel electrophoresis or DEAE-cellulose chromatography; the l...

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Detalles Bibliográficos
Autores principales: Nowicki, C., Montemartini, M., Duschak, V., Santomé, JosA., Cazzulo, J.J.
Formato: JOUR
Materias:
p-Hydroxyphenyl lactate dehydrogenase
Trypanosoma cruzi
Tyrosine aminotransferase
4 hydroxyphenyllactic acid
4-hydroxyphenyllactic acid
oxidoreductase
phenylpropionic acid derivative
tyrosine aminotransferase
aspartate aminotransferase
animal
article
cell cycle
cell fractionation
enzymology
isolation and purification
metabolism
ultrastructure
epimastigote
mitochondrion
nonhuman
priority journal
protein localization
trypanosoma cruzi
Animal
Cell Cycle
Oxidoreductases
Phenylpropionates
Subcellular Fractions
Support, Non-U.S. Gov't
Tyrosine Transaminase
Trypanosoma
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03781097_v92_n2_p119_Nowicki
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Cell-free extracts of epimastigotes of Trypanosoma cruzi contain tyrosine aminotransferase (TAT) and p-hydroxyphenyllactate dehydrogenase (pHPLDH). The TAT activity could be separated from aspartate aminotransferase (ASAT) by polyacrylamide gel electrophoresis or DEAE-cellulose chromatography; the latter procedure also allowed complete separation of pHPLDH. The subcellular localization of both T. cruzi enzymes, as determined by digitonin extraction, subcellular fractionation by differential centrifugation, and isopycnic ultracentrifugation in sucrose gradients, was mainly cytosolic, with low mitochondrial activities. © 1992.

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