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Effects of Temperature and Common Ions on Binding of Puerarin to BSA

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Abstract

The effects of temperature and common ions on binding of puerarin to bovine serum albumin (BSA) are investigated. The binding constants (K a) between puerarin and BSA are 1.13×104 L⋅mol−1 (20 °C) and 1.54×104 L⋅mol−1 (30 °C), and the number of binding sites (n) is (0.95±0.02). However, at a higher temperature (40 °C) the stability of the puerarin–BSA system decreases, which results in a lower binding constant (1.58×103 L⋅mol−1) and number of binding sites (n=0.73) of the puerarin–BSA system. However, the presence of Cu2+ and Fe3+ ions increases the binding constants and the number of binding sites in the puerarin–BSA complex.

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  1. School of Chemistry and Chemical Engineering, Nantong University, Nantong, Jiangsu, 226007, P.R. China

    Hui Cao & Quan Liu

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  1. Hui Cao
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  2. Quan Liu
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Correspondence to Quan Liu.

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Cao, H., Liu, Q. Effects of Temperature and Common Ions on Binding of Puerarin to BSA. J Solution Chem 38, 1071–1077 (2009). https://doi.org/10.1007/s10953-009-9430-3

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  • DOI: https://doi.org/10.1007/s10953-009-9430-3

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