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.
Lingua originaleEnglish
pagine (da-a)75-81
Numero di pagine7
RivistaItalian Journal of Biochemistry
Volume36
Stato di pubblicazionePubblicato - 1987

Keywords

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

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