Measurement of the Bovine Pancreatic Trypsin Inhibitors by Radioimmunoassay

  • E. Fink
  • L. J. Greene
Part of the Bayer-Symposium book series (BAYER-SYMP, volume 5)


Bovine pancreas contains two polypeptide trypsin inhibitors which are not homologous and differ in their inhibitory activity towards chymotrypsin, kallikrein, elastase and other serine proteinases [1]. The Kunitz inhibitor [2, 3] and the Kazal inhibitor [4, 5] are present in approximately equimolar concentrations in bovine pancreatic tissue [6], yet only the Kazal inhibitor is detectable in the pancreatic juice [6, 7]. The Kazal inhibitor has been named the pancreatic secretory trypsin inhibitor, PSTI [8] because its concentration in the pancreatic juice parallels that of the exocrine secretory proteins [7, 9, 10]. The Kunitz inhibitor is considered the “intracellular” inhibitor [7]. However, no direct information is available concerning the intracellular localization of these inhibitors in the pancreas. A sensitive and specific analytical method for the measurement of Kazal and Kunitz inhibitors at the picogram-nanogram level is required for intracellular distribution studies. The preparation of trace labelled 131I-Kunitz inhibitor by the chloramine T method and its use in a radioimmunoassay have been described by Arndts et al. [11]. In this communication we report the preparation of 125I derivatives of Kazal and Kunitz inhibitors by the lactoperoxidase method and present a radioimmunoassay for each inhibitor.


Trypsin Inhibitor Pancreatic Juice Brookhaven National Laboratory Bovine Pancreas Kunitz Trypsin Inhibitor 
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Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • E. Fink
    • 1
  • L. J. Greene
    • 1
  1. 1.Biology DepartmentBrookhaven National LaboratoryUptonUSA

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