Vitamin C-bovine serum albumin binding behaviour

Elisabetta Meucci Calabrese, G. E. Martorana, A. Ursitti, Giacinto Abele Donato Miggiano, Alvaro Mordente, A. Castelli

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4 Citations (Scopus)


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
Publication statusPublished - 1987


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


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