Enzymatic oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous α-amylase
✍ Scribed by Ekaterina L. Gvozdeva; Tatyana A. Valueva; Vladimir V. Mosolov
- Book ID
- 115928715
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 187 KB
- Volume
- 334
- Category
- Article
- ISSN
- 0014-5793
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📜 SIMILAR VOLUMES
We have cloned and sequenced a full-length cDNA from barley (Hordeum vulgate L.) seeds encoding the bifunctional ~-amylase/subtilisin inhibitor (BASI). The nucleotide sequence predicts an open reading frame coding for a protein of 203 amino acids. The first 22 amino acids exhibit the sequence charac
Polymorphism of an endogenous α-amylase inhibitor in wheat was studied using iso-electric focusing followed by monoclonal antibody - based immunoblotting. Ten isoforms of the inhibitor detected in common wheat and its wild counterparts were assigned to five homoeologous loci. Three α-amylase inhibit