Journal of Protein Chemistry

, Volume 14, Issue 6, pp 467–475 | Cite as

Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds

  • Eric Ferrasson
  • Laurence Quillien
  • Jacques Gueguen
Article

Abstract

Trypsin inhibitors from winter pea seeds (c.v. Frilene) have been purified by ammonium sulfate precipitation, gel filtration, and anion and cation exchange chromatography and shown to consist of six protease inhibitors (PSTI I, II, III, IVa, IVb, and V). Their molecular weights were determined by electrospray mass spectrometry as 6916, 6807, 7676, 7944, 7848, and 7844 D, respectively, and the sequences of the first 20 N-terminal amino acid residues of these six inhibitors were found to be identical. The complete amino acid sequence of PSTI IVa was determined. This protein comprises a total of 72 residues and has 14 cysteines, all involved in disulfide bridges. Comparison of the sequence of PSTI IVa with those of other leguminous Bowman-Birk type inhibitors revealed that PSTI could be classified as a group III inhibitor, closely related toVicia faba andVicia angustifolia inhibitors.

Key words

Trypsin inhibitor Pisum sativum amino acid sequence Bowman-Birk type inhibitors 

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Copyright information

© Plenum Publishing Corporation 1995

Authors and Affiliations

  • Eric Ferrasson
    • 1
  • Laurence Quillien
    • 1
  • Jacques Gueguen
    • 1
  1. 1.Laboratoire de Biochimie et Technologie des ProtéinesINRA NantesNantes Cedex 03France

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