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
Solvent perturbation spectra of yellow mealworm α-amylase and of wheat protein inhibitors
✍ Scribed by L. Vittozzi; G. De Angelis; V. Silano
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 412 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0020-711X
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