Assignment of the five disulfide bridges in an alpha-amylase inhibitor from wheat kernel by fast-atom-bombardment mass spectrometry and Edman degradation.

@article{Poerio1991AssignmentOT,
  title={Assignment of the five disulfide bridges in an alpha-amylase inhibitor from wheat kernel by fast-atom-bombardment mass spectrometry and Edman degradation.},
  author={Elia Poerio and Carlo Caporale and L{\`u}cia Carrano and P. Pucci and Vincenzo Buonocore},
  journal={European journal of biochemistry},
  year={1991},
  volume={199 3},
  pages={595-600}
}
The assignment of the five disulfide bridges in an alpha-amylase monomeric inhibitor from wheat kernel (coded 0.28) was achieved by combining fast-atom-bombardment mass spectrometry (FAB-MS) and automatic sequencing based on Edman degradation. Direct FAB-MS analysis of the native and reduced enzymatic digests of the protein allowed the assignment of three disulfide bridges out of five, including those involving two adjacent cysteine residues. The remaining two disulfide bridges were assigned by… CONTINUE READING