Nucleotide sequence of a cDNA coding for the barley seed protein CMa: an inhibitor of insect α-amylase

Research output: Contribution to journalJournal articleResearchpeer-review

  • Søren K. Rasmussen
  • Anette Johansson

The primary structure of the insect α-amylase inhibitor CMa of barley seeds was deduced from a full-length cDNA clone pc43F6. Analysis of RNA from barley endosperm shows high levels 15 and 20 days after flowering. The cDNA predicts an amino acid sequence of 119 residues preceded by a signal peptide of 25 amino acids. Ala and Leu account for 55% of the signal peptide. CMa is 60-85% identical with α-amylase inhibitors of wheat, but shows less than 50% identity to trypsin inhibitors of barley and wheat. The 10 Cys residues are located in identical positions compared to the cereal inhibitor family with a Pro-X-Cys motif present in all.

Original languageEnglish
JournalPlant Molecular Biology
Issue number2
Pages (from-to)423-427
Number of pages5
Publication statusPublished - 1 Jan 1992

    Research areas

  • CM protein, Hordeum vulgare L., wheat

ID: 204471338