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The specificity of proanthocyanidin-protein interactions.
Open accessAbstract
The proanthocyanidins or condensed tannins, phenolic polymers which are synthesized by many plants, characteristically bind and precipitate proteins. The specificity of the interaction was investigated using a competitive binding assay to compare directly the affinities of various proteins and synthetic polymers for the tannin obtained from Sorghum bicolor (Lin.) Moench. At pH 4.9, the relative affinities range over more than 4 orders of magnitude, indicating that this proanthocyanidin interacts quite selectively with protein and protein-like polymers. The affinity for tannins is an inverse function of the size of the polymer, and peptides with less than six residues interact very weakly with tannin. Proteins are precipitated by proanthocyanidins most efficiently at pH values near their isoelectric points. Proline-rich proteins and polymers have very high affinities for tannin. Tightly coiled globular proteins have much lower affinities for tannin than conformationally loose proteins.
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Cited by
Structure-antioxidant activity relationships of flavonoids and phenolic acids
Rice-Evans, C. A., Miller, N. J., & Paganga, G. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02227-9 · Cited by 9,085
Tannins and Human Health: A Review
Chung, K.-T., Wong, T. Y., Wei, C.-I., Huang, Y.-W., & Lin, Y. (1998) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408699891274273 · Cited by 1,996
Santos-Buelga, C., & Scalbert, A. (2000) · Journal of the Science of Food and Agriculture · doi:10.1002/(sici)1097-0010(20000515)80:7<1094::aid-jsfa569>3.0.co;2-1 · Cited by 1,258
Min, B. R., Barry, T. N., Attwood, G. T., & McNabb, W. C. (2003) · Animal Feed Science and Technology · doi:10.1016/s0377-8401(03)00041-5 · Cited by 1,051
Sorghum phytochemicals and their potential impact on human health
Awika, J. M., & Rooney, L. W. (2004) · Phytochemistry · doi:10.1016/j.phytochem.2004.04.001 · Cited by 966
Metadata
- Authors
- Hagerman, A. E., & Butler, L. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-05
- Volume
- 256
- Issue
- 9
- Pages
- 4494-4497
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1513215086
- Cited by
- 1,000
- References
- 0
- FWCI
- 16.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
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