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

Role of tryptophan, histidine and methionine residues in the catalytic activity of mitochondrial aspartate aminotransferase from beef kidney / G., Polidoro; D., Di Cola; C., Di Ilio; G., Del Boccio; Politi, Laura; Scandurra, Roberto. - In: PHYSIOLOGICAL CHEMISTRY AND PHYSICS. - ISSN 0031-9325. - 7:3(1975), pp. 255-261.

Role of tryptophan, histidine and methionine residues in the catalytic activity of mitochondrial aspartate aminotransferase from beef kidney.

POLITI, Laura;SCANDURRA, Roberto
1975

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
1975
01 Pubblicazione su rivista::01a Articolo in rivista
Role of tryptophan, histidine and methionine residues in the catalytic activity of mitochondrial aspartate aminotransferase from beef kidney / G., Polidoro; D., Di Cola; C., Di Ilio; G., Del Boccio; Politi, Laura; Scandurra, Roberto. - In: PHYSIOLOGICAL CHEMISTRY AND PHYSICS. - ISSN 0031-9325. - 7:3(1975), pp. 255-261.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/465783
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