Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (itBrassica napus) seed

Fabrizio Ceciliani, Fabrizio Bortolotti, Enea Menegatti, Severino Ronchi, Paolo Ascenzi, Sandro Palmieri

Research output: Contribution to journalArticlepeer-review

Abstract

A new serine proteinase inhibitor, rapeseed trypsin inhibitor (RTI), has been isolated from rapeseed (Brassica napus var. oleifera) seed. The protein inhibits the catalytic activity of bovine β-trypsin and bovine α-chymotrypsin with apparent dissociation constants of 3.0 × 10-10 M and 4.1 × 10-7 M, at pH 8.0 and 21°C, respectively. The stoichiometry of both proteinase-inhibitor complexes is 1:1. The amino acid sequence of RTI consists of 60 amino acid residues, corresponding to an Mr, of about 6.7 kDa. The p1-pi, reactive site bond has been tentatively identified at position Arg20-Ile21. RTI shows no similarity to other serine proteinase inhibitors except the low molecular weight mustard trypsin inhibitor (MTI-2). RTI and MTI-2 could be members of a new class of plant serine proteinase inhibitors.

Original languageEnglish
Pages (from-to)221-224
Number of pages4
JournalFEBS Letters
Volume342
Issue number2
DOIs
Publication statusPublished - Apr 4 1994

Keywords

  • Amino acid sequence
  • Brassica napus var. oleifera
  • Rapeseed
  • Serine proteinase inhibitor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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