PMID: 7537103Apr 13, 1995Paper

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

Biochimica Et Biophysica Acta
L FiorucciF Ascoli

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.

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Citations

Oct 27, 1998·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·L FiorucciF Ascoli
Apr 17, 1995·FEBS Letters·L FiorucciF Ascoli
May 14, 1998·The Journal of Laboratory and Clinical Medicine·H KobayashiT Terao
Dec 31, 1997·Archives of Biochemistry and Biophysics·L FiorucciF Ascoli
May 29, 2003·Biophysical Journal·Michael GottschalkBertil Halle
Mar 10, 2000·Biochimica Et Biophysica Acta·C P SommerhoffH Fritz

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