title: Conformational changes of serum albumin induced by ascorbic acid.
abstract: Bovine serum albumin (BSA) was found to inhibit the autooxidation of ascorbic acid (AA) at physiologic pH. The spontaneous oxidation rate of AA at 1 X 10(-5) M was 0.87 mumol X L-1 min-1. In the presence of 1 microM BSA, the rate is 15% of the spontaneous rate (0.13 mumol X L-1 X min-1). The u.v. difference spectrum of the AA:BSA complex reveals a decrease in absorbance at 204 nm. These data provide evidence that AA binds to BSA and induces a conformational change in the BSA molecule.
mesh_terms: D000818:Animals; D001205:Ascorbic Acid / Q000097:blood*; D002417:Cattle; D007700:Kinetics; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
chemical_list: D012710:Serum Albumin, Bovine; D001205:Ascorbic Acid