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  • Title: Role of tryptophan, histidine and methionine residues in the catalytic activity of mitochondrial aspartate aminotransferase from beef kidney.
    Author: Polidoro G, di Cola D, di Ilio C, del Boccio G, Politi L, Scandurra R.
    Journal: Physiol Chem Phys; 1975; 7(3):255-61. PubMed ID: 1187815.
    Abstract:
    The role of tryptophan, methionine, and histidine residues in mitochondrial aspartate aminotransferase from beef kidney has been established by using N-bromosuccinimide, 2-hydroxy-5-nitrobenzylbromide, and tetraiodofluoresceine as specific chemical modifiers of the amino acid residues of the enzyme. Since N-bromosuccinimide promotes extensive inactivation of the enzyme and the chemical modification of 1.65 tryptophan and 3 methionine residues per enzymes protomer, 2-hydroxy-5-nitrobenzylbromide modifies once more 1.65 tryptophan residues per enzyme protomer but induces only 10% inactivation of the enzyme. Tetraiodofluoresceine exerts a 40% inactivation of the enzyme which is due to the chemical modification of 5.8 histidine res in
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