Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442- and Val561-plasmin: a comparative study

Paolo Ascenzi, Gino Amiconi, Martino Bolognesi, Enea Menegatti, Mario Guarneri

Research output: Contribution to journalArticle

Abstract

Thermodynamic and kinetic parameters for the binding of the bovine basic bancreatic trypsin inhibitor (BPTI, Kunitz inhibitor) to human Glu1-, Lys77-, Val442- and Val561-plasmin (EC 3.4.21.7) have been determined between pH 3.0 and 9.5, and from 5.0 to 45.0°C. The inhibitor-binding properties to human Glu1-, Lys77-, Val442-and Val561-plasmin suggest a possible role of BPTI in modulating plasmin activity when the inhibitor is used therapeutically.

Original languageEnglish
Pages (from-to)134-136
Number of pages3
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1040
Issue number1
DOIs
Publication statusPublished - Aug 1 1990

Keywords

  • (Bovine trypsin inhibitor)
  • (Human plasmin)
  • Basic pancreatic trypsin inhibitor
  • inhibitor complex formation
  • Kinetics
  • Kunitz inhibitor
  • Proteinase
  • Thermodynamics

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

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