Conformational changes of serum albumin induced by ascorbic acid
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 22 (5) , 565-567
- https://doi.org/10.1111/j.1399-3011.1983.tb02129.x
Abstract
Bovine serum albumin (BSA) inhibited the autooxidation of ascorbic acid (AA) at physiologic pH. The spontaneous oxidation rate of AA at 1 .times. 10-5 M was 0.87 .mu.mol .cntdot. l-1 min-1. In the presence of 1 .mu.M BSA, the rate is 15% of the spontaneous rate (0.13 .mu.mol .cntdot. l-1 .cntdot. min-1). The UV difference spectrum of the AA:BSA complex reveals a decrease in absorbance at 204 nm. AA probably binds to BSA and induces a conformational change in the BSA molecule.Keywords
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