Bifunctional a-amylase/subtilisin inhibitors have been implicated in plant defence and regulation of endogenous a-amylase action. The barley a-amylase/subtilisin inhibitor (BASI) inhibits the barley a-amylase 2 (AMY2) and subtilisin-type serine proteases. BASI belongs to the Kunitz-type trypsin inhi
Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization
✍ Scribed by John Mundy; IB Svendsen; Jørn Hejgaard
- Publisher
- Springer-Verlag
- Year
- 1983
- Weight
- 1005 KB
- Volume
- 48
- Category
- Article
- ISSN
- 0105-1938
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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
Changes in bifunctional alpha-amylase/subtilisin inhibitor (BASI) expression induced by abscisic acid (ABA) were studied using in vitro cultured barley (Hordeum vulgare cv. Bonanza) embryos. The steady-state levels of BASI mRNA and BASI protein were increased by exogenously applied ABA. Accumulation