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Journal article

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

From

Risø National Laboratory for Sustainable Energy, Technical University of Denmark1

The primary structure of the insect alpha-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 alpha-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.

Language: English
Publisher: Kluwer Academic Publishers
Year: 1992
Pages: 423-427
Journal subtitle: An International Journal on Molecular Biology, Molecular Genetics and Biochemistry
ISSN: 15735028 and 01674412
Types: Journal article
DOI: 10.1007/BF00034972
ORCIDs: 0000-0001-6169-2504

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