Trypsin Complexed with α1-Proteinase Inhibitor Has an Increased Structural Flexibility

  • Gyula Kaslik
  • András Patthy
  • Miklós Bálint
  • László Gráf


Mutant rat trypsin Asp189 Ser was prepared and complexed with highly purified human α1 -proteinase inhibitor. The complex formed was purified to homogeneity and studied by N-terminal amino acid sequence analysis and limited proteolysis with bovine trypsin. As compared to uncomplexed mutant trypsin the mutant enzyme complexed with α1 -proteinase inhibitor showed a highly increased susceptibility to enzymatic digestion. The peptide bond selectively attacked by bovine trypsin was identified as the Arg117 — Val118 one of trypsin. The structural and mechanistic relevance of this observation to serine proteinase-substrate and serine proteinase-serpin reactions are discussed.


Limited Proteolysis Serine Proteinase Action Bovine Pancreatic Trypsin Inhibitor Bovine Trypsin Porcine Pancreatic Elastase 
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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Gyula Kaslik
    • 1
  • András Patthy
    • 2
  • Miklós Bálint
    • 1
  • László Gráf
    • 1
  1. 1.Department of BiochemistryEötvös UniversityBudapestHungary
  2. 2.Agricultural Biotechnology CenterGödöllõHungary

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