Very low amounts of ascorbic acid modify alkaline phosphatase fluorescence, absorption and enzymatic activity. A strong quenching of enzyme, tryptophan and tyrosine emission together with evident alterations of the protein absorption characteristics are observed. The catalytic activity inhibition probably reflects a perturbation of the active site environment due to the interaction of ascorbic acid with enzyme aminoacyl residues.

Martorana, G., Meucci, E., Miggiano, G., Mordente, A., Castelli, A., Interaction between alkaline phosphatase and ascorbic acid by fluorescence and absorption studies, <<ITALIAN JOURNAL OF BIOCHEMISTRY>>, 1983; 32 (4): 231-238 [http://hdl.handle.net/10807/9756]

Interaction between alkaline phosphatase and ascorbic acid by fluorescence and absorption studies

Meucci, Elisabetta;Mordente, Alvaro;
1983

Abstract

Very low amounts of ascorbic acid modify alkaline phosphatase fluorescence, absorption and enzymatic activity. A strong quenching of enzyme, tryptophan and tyrosine emission together with evident alterations of the protein absorption characteristics are observed. The catalytic activity inhibition probably reflects a perturbation of the active site environment due to the interaction of ascorbic acid with enzyme aminoacyl residues.
Inglese
Martorana, G., Meucci, E., Miggiano, G., Mordente, A., Castelli, A., Interaction between alkaline phosphatase and ascorbic acid by fluorescence and absorption studies, <<ITALIAN JOURNAL OF BIOCHEMISTRY>>, 1983; 32 (4): 231-238 [http://hdl.handle.net/10807/9756]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10807/9756
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