Primary Structure and Reactive Site of a Novel Wheat Proteinase Inhibitor of Subtilisin and Chymotrypsin

@inproceedings{Poerio2003PrimarySA,
  title={Primary Structure and Reactive Site of a Novel Wheat Proteinase Inhibitor of Subtilisin and Chymotrypsin},
  author={Elia Poerio and Stefano Di Gennaro and Antimo Di Maro and Francesca Farisei and Pasquale Ferranti and Augusto Parente},
  booktitle={Biological chemistry},
  year={2003}
}
Abstract The proteinase inhibitor WSCI, active in inhibiting bacterial subtilisin and a number of animal chymotrypsins, was purified from endosperm of exaploid wheat (Triticum aestivum, c.v. San Pastore) by ion exchange chromatography and its complete amino acid sequence was established by automated Edman degradation. WSCI consists of a single polypeptide chain of 72 amino acid residues, has a molecular mass of 8126.3 Da and a pI of 5.8. The inhibition constants (K1) for Bacillus licheniformis… CONTINUE READING

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