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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility

G Kaslik1, A Patthy, M Bálint

  • 1Department of Biochemistry, Eötvös University, Budapest, Hungary.

FEBS Letters
|August 21, 1995
PubMed
Summary

Mutant rat trypsin complexed with alpha 1-proteinase inhibitor showed increased susceptibility to digestion. Bovine trypsin selectively cleaved the Arg117-Val118 bond in the complexed mutant enzyme.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Proteinase Inhibitors

Background:

  • Serine proteinases play crucial roles in biological processes.
  • Serine proteinase inhibitors (serpins) regulate enzyme activity.
  • Understanding enzyme-inhibitor interactions is vital for molecular biology.

Purpose of the Study:

  • To investigate the structural and mechanistic consequences of complex formation between mutant rat trypsin and human alpha 1-proteinase inhibitor.
  • To identify specific cleavage sites in the enzyme-inhibitor complex.

Main Methods:

  • Preparation and purification of mutant rat trypsin (Asp189Ser).
  • Complex formation with human alpha 1-proteinase inhibitor.
  • N-terminal amino acid sequence analysis and limited proteolysis using bovine trypsin.

Main Results:

  • The mutant trypsin-alpha 1-proteinase inhibitor complex exhibited significantly higher susceptibility to enzymatic digestion compared to the uncomplexed mutant trypsin.
  • Bovine trypsin selectively cleaved the Arg117-Val118 peptide bond within the complexed mutant trypsin.

Conclusions:

  • Complexation with alpha 1-proteinase inhibitor alters the susceptibility of mutant rat trypsin to proteolysis.
  • The identified cleavage site provides insights into the structural dynamics of serine proteinase-serpin interactions.
  • This finding contributes to understanding the mechanisms of serine proteinase regulation.