Coenzyme active site occupancy as an indicator of independence of the subunits of mitochondrial aspartate aminotransferase.
Open Access
- 1 June 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (11) , 7003-7010
- https://doi.org/10.1016/s0021-9258(17)39829-0
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Specific labeling of the active site of cytosolic aspartate aminotransferase through the use of a cofactor analog N-(bromoacetyl)pyridoxamineBiochemistry, 1983
- Functional interactions between subunits of aspartate aminotransferaseJournal of Molecular Biology, 1982
- Interactions between apoaspartate aminotransferase and pyridoxal 5'-phosphate. A stopped-flow studyBiochemistry, 1981
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Itemizing enzyme ligand interactions in native and half-active hybrid aspartate transaminase to probe site-site relationsBiochemistry, 1976
- Large-Scale Purification and Some Properties of the Mitochondrial Aspartate Aminotransferase from Pig HeartEuropean Journal of Biochemistry, 1976
- Fluorinated amino acids and phosphopyridoxyl fluoroamino acids as reversible active site directed inhibitors of aspartate transaminaseBiochemical and Biophysical Research Communications, 1975
- The apo/holo hybrid of cytosolic aspartate aminotransferase, preparation and studies on subunit interactionsBiochemical and Biophysical Research Communications, 1974
- Reaction of cytoplasmic aspartate aminotransferase with tetranitromethaneBiochemistry, 1973
- Interaction between Pyridoxamine 5′‐Phosphate and Apo‐Aspartate Aminotransferase from Pig HeartEuropean Journal of Biochemistry, 1972