Structural studies of wheat monomeric and dimeric protein inhibitors of alpha-amylase.

@article{Petrucci1978StructuralSO,
  title={Structural studies of wheat monomeric and dimeric protein inhibitors of alpha-amylase.},
  author={Tamara Corinna Petrucci and Giovanni Sannia and R Parlamenti and Vittorio Silano},
  journal={The Biochemical journal},
  year={1978},
  volume={173 1},
  pages={229-35}
}
Two wheat monomeric protein inhibitors of alpha-amylase with mol.wt. 12000, designated inhibitors 0.28 and 0.39 according to their gel-electrophoretic mobilities, showed almost identical circular-dichroism spectra in both the far and near u.v. at different pH values as well as in the presence or absence of dissociating and reducing agents. Both inhibitors (0.28 and 0.39) were readily inactivated by reduction of the five disulphide bridges present in each inhibitor molecule. These properties are… CONTINUE READING

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