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

Biochim Biophys Acta. 1990 Aug 1;1040(1):134-6. doi: 10.1016/0167-4838(90)90157-b.

Abstract

Thermodynamic and kinetic parameters for the binding of the bovine basic pancreatic 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 degrees 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.

Publication types

  • Comparative Study

MeSH terms

  • Fibrinolysin / genetics
  • Fibrinolysin / metabolism*
  • Glutamine*
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lysine*
  • Mutation
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Thermodynamics
  • Trypsin Inhibitor, Kunitz Soybean / metabolism*
  • Trypsin Inhibitors / metabolism*
  • Valine*

Substances

  • Recombinant Proteins
  • Trypsin Inhibitors
  • Glutamine
  • Trypsin Inhibitor, Kunitz Soybean
  • Fibrinolysin
  • Valine
  • Lysine