The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris.
Open accessAbstract
Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of alpha-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal alpha-amylases, having no activity towards the corresponding plant, bacterial, and fungal enzymes, or any other hydrolytic enzyme tested. Optimal inhibitory activity is expressed during preincubation of enzyme and inhibitor at pH 5.5 and 37 degrees. Substrate prevents inhibition. Measurement of the stoichiometry on inhibition showed that a 1:1 complex of alpha-amylase and inhibitor is formed. Complex formation was demonstrated by chromatography on Sephadex G-100. The phaseolamin-amylase complex is dissociated at low pH values, apparently as a result of destruction of the enzyme; the complex cannot be dissociated by other conditions unfavorable for inhibition (low temperature or high pH). Phaseolamin inhibits hog pancreatic alpha-amylase in a noncompetitive manner.
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Cites
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Cell structure and starch nature as key determinants of the digestion rate of starch in legume
Würsch, P., Del Vedovo, S., & Koellreutter, B. (1986) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/43.1.25 · Cited by 271
Morton, R. L., Schroeder, H. E., Bateman, K. S., Chrispeels, M. J., Armstrong, E., & Higgins, T. J. V. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070054597 · Cited by 262
Viguiliouk, E., Blanco Mejia, S., Kendall, C. W. C., & Sievenpiper, J. L. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13312 · Cited by 101
Metadata
- Authors
- Marshall, J., & Lauda, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1975-10
- Volume
- 250
- Issue
- 20
- Pages
- 8030-8037
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1562255636
- Cited by
- 279
- References
- 19
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Marshall, J., & Lauda, C. (1975). Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)40811-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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