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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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Barley α-amylase/subtilisin inhibitor: s
✍ Peter K. Nielsen; Birgit C. Bønsager; Kenji Fukuda; Birte Svensson 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 437 KB

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

The bifunctional α-amylase/subtilisin in
✍ Robert Leah; John Mundy 📂 Article 📅 1989 🏛 Springer 🌐 English ⚖ 930 KB

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

Post-transcriptional regulation of bifun
✍ Jin-Hao Liu; Robert D. Hill 📂 Article 📅 1995 🏛 Springer 🌐 English ⚖ 579 KB

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