Polypeptide Chain Structure of Inter-α-Trypsin Inhibitor and Pre-α-Trypsin Inhibitor: Evidence for Chain Assembly by Glycan and Comparison with other “Kunin”-Containing Proteins

  • Jan J. Enghild
  • Ida B. Thørgersen
  • Salvatore V. Pizzo
  • Guy Salvesen
Part of the NATO ASI Series book series (NSSA, volume 191)


Proteins structurally related to the proteinase inhibitor aprotinin, systematically known as pancreatic trypsin inhibitor (Kunitz), occur in animals from a variety of orders including mammals, moluscs and coelenterates.1 The wide distribution of these proteins suggests that the ancestral gene is very old, at least as old as the radiation of multicellular animals.2


Sodium Dodecyl Sulfate Human Epidermal Growth Factor Receptor Heavy Chain Trypsin Inhibitor Horseshoe Crab 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Jan J. Enghild
    • 1
  • Ida B. Thørgersen
    • 1
  • Salvatore V. Pizzo
    • 1
  • Guy Salvesen
    • 1
  1. 1.From the Department of PathologyDuke University Medical CenterDurhamUSA

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