The complete amino acid sequence of a major wheat protein inhibitor of α-amylase
✍ Scribed by Nizar Kashlan; Michael Richardson
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 380 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0031-9422
No coin nor oath required. For personal study only.
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Protein α-amylase inhibitors extracted with water from seeds of a number of Triticum and Aegilops species were characterized according to their molecular weights and action specificities towards human salivary and Tenebrio molitor L. α-amylases. Four inhibitor peaks, with molecular weights 60000, 44
The amylase-protein amylase inhibitor system offers a unique model of specific and reversilbe protein-protein interaction. The monomeric and dimeric inhibitors, exhibiting closely related properties and interacting with the same amylase, also provide a convenient test to compare effects of monomer-m
The grain of six winter and spring wheat varicties, harvested in 1987, differing in baking quality were included in the study. A number of technological analysis were performed. Albumins, globulins and gliadins were washed out. The location of inhibitory activities in extracted proteins, against a-a