The amino acid sequence of a Bowman-Birk type proteinase inhibitor from faba beans (Vicia faba L.)

J Biochem. 1991 Dec;110(6):951-5. doi: 10.1093/oxfordjournals.jbchem.a123695.

Abstract

The amino acid sequence of a Bowman-Birk type proteinase inhibitor (FBI) from seeds of faba bean (Vicia faba L.) was determined by analysis of peptide fragments generated by reduction and S-carboxymethylation of enzymatically modified inhibitors, which were obtained from native FBI by limited proteolysis with TPCK-trypsin or TLCK-chymotrypsin at pH 3.5. The established sequence showed that FBI is highly homologous with Vicia angustifolia inhibitor (VAI0 but lacks the portion corresponding to the C-terminal 9 amino acids of VAI. The trypsin reactive-site peptide bond in FBI was also indicated to be Lys(16)-Ser(17) and the chymotrypsin reactive-site peptide bond to be Tyr(42)-Ser(43) by limited proteolysis with TPCK-trypsin or TLCK-chymotrypsin and by sequence comparison with other Bowman-Birk type inhibitors.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Fabaceae / chemistry*
  • Molecular Sequence Data
  • Plants, Medicinal*
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / isolation & purification
  • Sequence Homology, Nucleic Acid

Substances

  • Protease Inhibitors