| Autor: |
Yang F; Department of Biology, College of Life & Environment Science, Shanghai Normal University, 100 Guilin Rd, Shanghai 200234, PR China., Zhao Y, Kai G, Xiao J |
| Jazyk: |
angličtina |
| Zdroj: |
Food & function [Food Funct] 2011 Feb; Vol. 2 (2), pp. 137-41. Date of Electronic Publication: 2011 Jan 12. |
| DOI: |
10.1039/c0fo00092b |
| Abstrakt: |
The molecular property-affinity relationship of dietary flavonoids for bovine gamma-globulin (γ-globulin) was investigated by fluorescence titration analysis. The quenching effects of flavonoids on γ-globulin fluorescence depended on the structures of flavonoids. The magnitudes of binding constants between flavonoids and γ-globulin were within the range of 10(3)-10(5) L mol(-1). These data were much smaller than the affinities between flavonoids and purified bovine and human serum albumins. The affinities of flavonoids for γ-globulin were strongly influenced by the structural differences of the compounds under study. The affinities for γ-globulin decreased with increasing partition coefficients and increased with increasing hydrogen bond acceptor numbers of flavonoids, which suggested that the binding interaction was mainly caused by hydrogen bond forces. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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