Reaction of cytoplasmic aspartate aminotransferase with tetranitromethane
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00739a016
Reference32 articles.
1. The Molecular Weight and other Properties of Aspartate Aminotransferase from Pig Heart Muscle
2. Chemical evidence for syncatalytic conformational changes in aspartate aminotransferase
3. Syncatalytic modification of cytoplasmic aspartate aminotransferase: Identification of a peptide containing the modified cysteinyl residue
4. Cytoplasmic Aspartate Aminotransferase: Syncatalytic Sulfhydryl Group Modification
5. Selective modification of tyrosine and cysteine residues in aspartate aminotransferase from pig heart cytosol
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2. Modification and Inactivation of Rhodanese by 2,4,6-Trinitrobenzenesulphonic Acid;Journal of Enzyme Inhibition;1988-01
3. Coenzyme active site occupancy as an indicator of independence of the subunits of mitochondrial aspartate aminotransferase.;Journal of Biological Chemistry;1984-06
4. A spin label substrate analogue as active site-directed modifying agent. Tryptophan 140 of aspartate aminotransferase.;Journal of Biological Chemistry;1983-02
5. Modification of Trytophanase with Tetranitromethane;European Journal of Biochemistry;1981-10
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