Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi

An aromatic L-α-hydroxyacid dehydrogenase (AHADH) was purified to homogeneity from epimastigotes of Trypanosoma cruzi by a method involving chromatography on DEAE-cellulose, hydrophobic interaction chromatography on Phenyl-Sepharose and affinity chromatography on Affi-Gel Blue. The purified enzyme s...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Montemartini, M., Santomé, JosA., Cazzulo, J.J., Nowicki, C.
Formato: JOUR
Materias:
Amino acid catabolism
Aromatic amino acid
Aromatic hydroxyacid
Dehydrogenase
Epimastigote
Trypanosoma cruzi
oxidoreductase
animal experiment
article
controlled study
enzyme analysis
enzyme purification
epimastigote
nonhuman
priority journal
protein degradation
trypanosoma cruzi
Alcohol Oxidoreductases
Amino Acid Sequence
Amino Acids
Animal
Comparative Study
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Molecular Structure
Molecular Weight
Sequence Homology, Amino Acid
Substrate Specificity
Support, Non-U.S. Gov't
Animalia
Trypanosoma
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_01666851_v68_n1_p15_Montemartini
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

Ejemplares similares

Ejemplares similares