Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human α-, β- and γ-thrombin; a kinetic and thermodynamic study

Paolo Ascenzi, Massimo Coletta, Gino Amiconi, Raimondo de Cristofaro, Martino Bolognesi, Mario Guarneri, Enea Menegatti

Research output: Contribution to journalArticlepeer-review

Abstract

Kinetic and thermodynamic parameters for the binding of the bovine basic pancreatic trypsin inhibitor (BPTI, Kunitz inhibitor) to human α-, β- and γ-thrombin have been determined, between 5 and 45°C, at pH 7.5. BPTI-binding properties to human thrombins have been analyzed in parallel with those of serine (pro)enzymes acting on cationic and non-cationic substrates, with particular reference to the bovine β-trypsin/BPTI system. The observed binding behaviour of BPTI to human α-, β- and γ-thrombin has been related to the inferred stereochemistry of the enzyme/inhibitor contact region(s).

Original languageEnglish
Pages (from-to)156-161
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume956
Issue number2
DOIs
Publication statusPublished - Sep 21 1988

Keywords

  • (Bovine pancreas)
  • (Enzyme kinetics)
  • Enzyme inhibitor binding
  • Kunitz inhibitor
  • Thrombin
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

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