Binding of the trypsin inhibitor from white mustard (sinapis Alba L.) seeds to bovine βtrypsin: Thermodynamic study

Enea Menegatti, Marisa Boggian, Paolo Ascenzi, Pier Luigi Luisi

Research output: Contribution to journalArticlepeer-review

Abstract

The effect of pH and temperature on the association equilibrium constant (Ka) for the binding of the trypsin inhibitor from white mustard (Sinapis alba L.) seeds (MTI) to bovine βtrypsin (EC 3.4.21.4) has been investigated. On lowering the pH from 9 to 3, values of Ka for MTI binding to bovine βtrypsin decrease thus reflecting the acid-pK and-midpoint shifts, upon inhibitor association, of two independent ionizable groups, and of a three-proton transition, respectively. At pH 8.0, values of thermodynamic parameters for MTI binding to bovine βtrypsin are: Ka = 4.5 × 108M-1, ΔG° = - 11.6kcal/mol, and ΔS° = +53 entropy units (all at 21°C); and ΔH° = + 4.1 kcal/mol (temperature independent between 5°C and 45°C). Binding properties of MTI to bovine βtrypsin have been analyzed in parallel with those concerning macromolecular inhibitor association to serine (pro)enzymes.

Original languageEnglish
Pages (from-to)67-71
Number of pages5
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Volume2
Issue number1
DOIs
Publication statusPublished - 1987

Keywords

  • Bovine βtrypsin
  • Bovine βtrypsin:MTI complex formation
  • PH effects (on bovine βtrypsin: MTI complex formation)
  • Thermodynamics (of bovine βtrypsin MTI adduct formation)
  • Trypsin inhibitor (from white mustard Sinapis alba L., seeds)

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology
  • Biochemistry
  • Molecular Medicine

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