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 |
|---|---|
| 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