The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Interaction of Flavonoids with Bovine Serum Albumin: A Fluorescence Quenching Study
Abstract
The interaction between four flavonoids (catechin, epicatechin, rutin, and quercetin) and bovine serum albumin (BSA) was investigated using tryptophan fluorescence quenching. Quenching constants were determined using the Stern-Volmer equation to provide a measure of the binding affinity between the flavonoids and BSA. The binding affinity was strongest for quercetin and ranked in the order quercetin > rutin > epicatechin = catechin. The pH in the range of 5-7.4 does not affect significantly (p < 0.05) the association of rutin, epicatechin, and catechin with BSA, but quercetin exhibited a stronger affinity at pH 7.4 than at lower pH (p < 0.05). Quercetin has a total quenching effect on BSA tryptophan fluorescence at a molar ratio of 10:1 and rutin at approximately 25:1. However, epicatechin and catechin did not fully quench tryptophan fluorescence over the concentration range studied. Furthermore, the data suggested that the association between flavonoids and BSA did not change molecular conformation of BSA and that hydrogen bonding, ionic, and hydrophobic interaction are equally important driving forces for protein-flavonoid association.
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Recent developments in the detection of bovine serum albumin
Jahanban-Esfahlan, A., Ostadrahimi, A., Jahanban-Esfahlan, R., Roufegarinejad, L., Tabibiazar, M., & Amarowicz, R. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.07.096 · Cited by 304
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Metadata
- Authors
- Papadopoulou, A., Green, R. J., & Frazier, R. A.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-12-16
- Volume
- 53
- Issue
- 1
- Pages
- 158-163
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2052230935
- Cited by
- 960
- References
- 17
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- closed
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