Journal article
Nucleotide sequence of a cDNA coding for the barley seed protein CMa: an inhibitor of insect α-amylase
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 |
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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 |
Amino Acid Sequence Animals Base Sequence Biochemistry, general Blotting, Northern CM protein CMa protein, barley Hordeum Hordeum vulgare L. Insecta Life Sciences Molecular Sequence Data Plant Pathology Plant Proteins Plant Sciences Protein Sorting Signals Seeds Sequence Alignment alpha-Amylases wheat