Abstract

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.
Original languageEnglish
Pages (from-to)75-81
Number of pages7
JournalItalian Journal of Biochemistry
Volume36
Publication statusPublished - 1987

Keywords

  • Ascorbic Acid
  • Dehydroascorbic Acid
  • Protein Binding
  • Protein Conformation
  • Serum Albumin, Bovine

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