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Updated: Jul 30, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
Published on: May 25, 2018
Selective inhibition of trypsins by insect peptides: role of P6-P10 loop
C Kellenberger1, G Ferrat, P Leone
1Centre d'Immunologie de Marseille-Luminy, UMR 145, Parc Scientifique et Technologique de Luminy, Case 906, 13009 Marseille, France. kellenberger@ciml.univ-mrs.fr
Abstract:
PMP-D2 and HI, two peptides from Locusta migratoria, were shown to belong to the family of tight-binding protease inhibitors. However, they interact weakly with bovine trypsin (K(i) around 100 nM) despite a trypsin-specific Arg at the primary specificity site P1. Here we demonstrate that they are potent inhibitors of midgut trypsins isolated from the same insect and of a fungal trypsin from Fusarium oxysporum (K(i)

