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.
| Original language | English |
|---|---|
| Pages (from-to) | 231-238 |
| Number of pages | 8 |
| Journal | Italian Journal of Biochemistry |
| Volume | 32 |
| Issue number | 4 |
| Publication status | Published - 1983 |
All Science Journal Classification (ASJC) codes
- Biochemistry
Keywords
- Alkaline Phosphatase
- Animals
- Ascorbic Acid
- Cattle
- Fluorescence
- Kidney
- Spectrometry
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