Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology.

@article{Bernhard1989CoidentityOP,
  title={Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology.},
  author={W R Bernhard and Chris R Somerville},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={269 2},
  pages={695-7}
}
A class of small polypeptides, isolated from seeds of barley and millet, which had been previously identified as putative amylase inhibitors has been found to have striking amino acid sequence identity with phospholipid transfer proteins. In addition, both classes of proteins have the same molecular weight and appear to be produced by proteolytic cleavage of an amino-terminal peptide of similar size. These properties, and the lack of any known activity for the barley protein, suggest that the… CONTINUE READING