Calf intestinal alkaline phosphatase is inactivated by 2,3-butanedione and phenylglyoxal. The reaction with either reagent results in a biphasic loss of enzymatic activity. Inactivation by 2,3-butanedione in borate buffer can be reversed after gel-filtration in Tris buffer but no enzyme reactivation is observed after phenylglyoxal treatment. Phosphate, ATP and NADH protect the enzyme from both compounds while no protection is displayed by L-phenylalanine. The selective chemical modification indicates that two differently reacting types of arginines are present in the active site domains of the dimeric enzyme.

Miggiano, G., Mordente, A., Martorana, G., Castelli, A., Modification of arginine residues in calf intestinal alkaline phosphatase, <<ITALIAN JOURNAL OF BIOCHEMISTRY>>, 1985; 34 (5): 364-372 [http://hdl.handle.net/10807/9757]

Modification of arginine residues in calf intestinal alkaline phosphatase

Mordente, Alvaro;
1985

Abstract

Calf intestinal alkaline phosphatase is inactivated by 2,3-butanedione and phenylglyoxal. The reaction with either reagent results in a biphasic loss of enzymatic activity. Inactivation by 2,3-butanedione in borate buffer can be reversed after gel-filtration in Tris buffer but no enzyme reactivation is observed after phenylglyoxal treatment. Phosphate, ATP and NADH protect the enzyme from both compounds while no protection is displayed by L-phenylalanine. The selective chemical modification indicates that two differently reacting types of arginines are present in the active site domains of the dimeric enzyme.
1985
Inglese
Miggiano, G., Mordente, A., Martorana, G., Castelli, A., Modification of arginine residues in calf intestinal alkaline phosphatase, <<ITALIAN JOURNAL OF BIOCHEMISTRY>>, 1985; 34 (5): 364-372 [http://hdl.handle.net/10807/9757]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10807/9757
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