Primary structure and specificity of a serine proteinase inhibitor from paprika (Capsicum annuum) seeds

Nikolinka Antcheva, András Patthy, Alekos Athanasiadis, Bojidar Tchorbanov, Sotir Zakhariev, Sándor Pongor

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Several fractions demonstrating trypsin inhibitory activity were isolated from the seeds of the paprika plant (Capsicum annuum). One of the inhibitors, PSI-1.1, was purified to homogeneity and characterised. The mature form of PSI-1.1 has a molecular mass of 6053 Da and consists of 55 amino acids in a sequence showing over 80% identity with members of the inhibitors of potato-2 family. PSI-1.1 is a potent inhibitor of trypsin (K(i) = 4.8 · 10-10 M) and a somewhat weaker inhibitor of chymotrypsin (K(i) = 4.7 · · 10-8 M) and pronase E (K(i) = 5.9 · 10-8 M). PSI-1.1 is resistant to heat up to 85°C, to acidic conditions (down to pH 2.0) and to pepsin digestion, presumably due to its four disulfide bridges.

Original languageEnglish
Pages (from-to)95-101
Number of pages7
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1298
Issue number1
DOIs
Publication statusPublished - Nov 14 1996

Keywords

  • Capsicum annuum
  • Primary structure
  • Proteinase inhibitor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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