Distinctions in the Equilibrium Kinetic Constants of the Mitochondrial and Supernatant Isozymes of Aspartate Transaminase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
1. A Kinetic and Equilibrium Analysis of the Glutamic Oxaloacetate Transaminase Mechanism
2. Isolation and Characterization of Multiple Forms of Glutamate-Aspartate Aminotransferase from Pig Heart
3. Kinetic Studies of Glutamic Oxaloacetic Transaminase Isozymes*
4. Kinetics and Electrophoretic Properties of the Isozymes of Aspartate Aminotransferase from Pig Heart
5. Immunochemical and Kinetic Properties of Anionic and Cationic Glutamic-Oxaloacetic Transaminases Separated from Human Heart and Human Liver
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2. THE PHOSPHOPYRIDOXYL PEPTIDE FROM THE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE OF BEEF KIDNEY;International Journal of Peptide and Protein Research;2009-01-12
3. Tautomerism in Pyridoxal Phosphate and in Enzymatic Catalysis;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
4. Phosphonate Analogues of α-Ketoglutarate Inhibit the Activity of the α-Ketoglutarate Dehydrogenase Complex Isolated from Brain and in Cultured Cells;Biochemistry;2005-07-15
5. Use of 1H−15N Heteronuclear Multiple-Quantum Coherence NMR Spectroscopy To Study the Active Site of Aspartate Aminotransferase;Biochemistry;1997-01-01
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