TY - JOUR
T1 - Vitamin C-bovine serum albumin binding behaviour
AU - Meucci Calabrese, Elisabetta
AU - Martorana, G. E.
AU - Ursitti, A.
AU - Miggiano, Giacinto Abele Donato
AU - Mordente, Alvaro
AU - Castelli, A.
PY - 1987
Y1 - 1987
N2 - 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.
AB - 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.
KW - Ascorbic Acid
KW - Dehydroascorbic Acid
KW - Protein Binding
KW - Protein Conformation
KW - Serum Albumin, Bovine
KW - Ascorbic Acid
KW - Dehydroascorbic Acid
KW - Protein Binding
KW - Protein Conformation
KW - Serum Albumin, Bovine
UR - http://hdl.handle.net/10807/9754
M3 - Article
SN - 0021-2938
VL - 36
SP - 75
EP - 81
JO - Italian Journal of Biochemistry
JF - Italian Journal of Biochemistry
ER -