Localization and interaction of bovine pancreatic trypsin inhibitor and tryptase in the granules of bovine mast cells

Laura Fiorucci, Fulvio Erba, Laura Falasca, Luciana Dini, Franca Ascoli

Research output: Contribution to journalArticlepeer-review

Abstract

The interaction of bovine pancreatic trypsin inhibitor and bovine tryptase, isolated from liver capsule mast cells, was investigated. They form a complex in vitro with a Ki of 5.6 nM at pH 8.0 and are localized within the mast cell granules, as shown by immunogold staining at the electron microscope level. In addition, double immunogold electron microscopy revealed that the inhibitor and the enzyme are present in the same granules, where they occur in clusters; this may be taken as an indication of their interaction in vivo and suggests a physiological role for bovine pancreatic trypsin inhibitor in the regulation of tryptase proteolytic activity.

Original languageEnglish
Pages (from-to)407-413
Number of pages7
JournalBBA - General Subjects
Volume1243
Issue number3
DOIs
Publication statusPublished - Apr 13 1995

Keywords

  • BPTI
  • Localization
  • Mast cell
  • Serine protease
  • Tryptase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Localization and interaction of bovine pancreatic trypsin inhibitor and tryptase in the granules of bovine mast cells'. Together they form a unique fingerprint.

Cite this