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.
Lingua originale | English |
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pagine (da-a) | 231-238 |
Numero di pagine | 8 |
Rivista | Italian Journal of Biochemistry |
Volume | 32 |
Stato di pubblicazione | Pubblicato - 1983 |
Keywords
- Alkaline Phosphatase
- Animals
- Ascorbic Acid
- Cattle
- Kidney
- Spectrometry, Fluorescence