Magnetic resonance relaxation rates in the study of complexes of ligands with spin-labeled aspartate transaminase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Glutamic-Aspartic Transaminase
2. Distinctions in the Equilibrium Kinetic Constants of the Mitochondrial and Supernatant Isozymes of Aspartate Transaminase
3. The Mechanism of Transamination
4. THE SITE OF BINDING OF PYRIDOXAL-5'-PHOSPHATE TO HEAR GLUTAMIC-ASPARTIC TRANSAMINASE
5. Cytoplasmic Aspartate Aminotransferase: Syncatalytic Sulfhydryl Group Modification
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Binding to phospholipid vesicles impairs substrate-mediated conformational changes of the precursor to mitochondrial aspartate aminotransferase.;Journal of Biological Chemistry;1994-09
2. Methyl methanethiosulfonate as an active site probe of serine hydroxymethyltransferase.;Journal of Biological Chemistry;1982-10
3. Substrate-mediated increased reactivity of a critical sulfhydryl group of crystals of cytoplasmic aspartate transaminase;Archives of Biochemistry and Biophysics;1980-07
4. Stereochemistry of holoaspartate transaminase after modification of the active site Lys-258.;Journal of Biological Chemistry;1979-05
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