A comparative study of the thermal inactivation of cytosolic and mitochondrial aspartate aminotransferases
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference25 articles.
1. The intracellular distribution, latency and electrophoretic mobility of l-glutamate-oxaloacetate transaminase from rat liver
2. Aspartate Aminotransferase Isozymes in Panicum miliaceum L, an NAD-Malic Enzyme-Type C4 Plant: Comparison of Enzymatic-Properties, Primary Structures, and Expression Patterns
3. The complete amino acid sequences of cytosolic and mitochondrial aspartate aminotransferases from horse heart, and inferences on evolution of the isoenzymes
4. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
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1. First cloning and characterization of aspartate aminotransferase from river buffalo (Bubalus bubalis);Biologia;2011-10-28
2. Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase;International Journal of Biological Macromolecules;2009-06
3. Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of α-crystallin;European Biophysics Journal;2009-01-27
4. Thermal inactivation, denaturation and aggregation of mitochondrial aspartate aminotransferase;Biophysical Chemistry;2008-06
5. Asymmetric synthesis of unnaturall-amino acids using thermophilic aromaticl-amino acid transaminase;Biotechnology and Bioprocess Engineering;2006-08
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