Complete amino acid sequence of the protease inhibitor from buckwheat seeds

FEBS Lett. 1995 Sep 11;371(3):264-6. doi: 10.1016/0014-5793(95)00899-k.

Abstract

The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da. The active site of the inhibitor contains an Arg45-Asp46 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the proteinase inhibitor I family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Edible Grain / chemistry*
  • Molecular Sequence Data
  • Plant Proteins / chemistry*
  • Seeds / chemistry
  • Trypsin Inhibitors / chemistry*

Substances

  • Amino Acids
  • BWI-1 protein, Fagopyrum esculentum
  • Plant Proteins
  • Trypsin Inhibitors