
pmid: 3597048
handle: 10807/9754
The binding of ascorbic acid and dehydroascorbic acid to bovine serum albumin is greatly heterogeneous. The Hill plots, as evaluated from the fluorescence quenching measurements, clearly show a biphasic behaviour. Scatchard analysis moreover indicates that the potency and the pattern of the binding can change gradually in the process of occupation of various sites because of albumin structural modifications.
Protein Conformation, Serum Albumin, Bovine, Ascorbic Acid, Dehydroascorbic Acid, Protein Binding
Protein Conformation, Serum Albumin, Bovine, Ascorbic Acid, Dehydroascorbic Acid, Protein Binding
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