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Updated: Aug 24, 2026

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
Published on: January 17, 2025
Reduction of active elastase concentration by means of immobilized inhibitors: a novel therapeutic approach
Valentina Grano1, Gianluca Tasco, Rita Casadio
1Department of Experimental Medicine, Second University of Naples, Via S. M. di Costantinopoli 16, 80138 Naples, Italy.
Abstract:
The inhibitory power of three different active Nylon membranes, separately loaded with three different protease inhibitors, was studied with the aim of reducing the increased elastase concentration occurring during hemodialysis or extracorporeal blood circulation in patients undergoing cardiopulmonary bypass. Chemical grafting was carried out to make the inert Nylon membrane suitable for the immobilization of the inhibitors. The behavior of immobilized alpha(1)-antitrypsin, bovine pancreatic trypsin inhibitor (BPTI), or elastatinal was separately studied. alpha(1)-Antitrypsin and BPTI were covalently immobilized by means of a diazotization process, whereas elastatinal was covalently attached via a condensation process mediated by glutaraldehyde. The inhibitory power of each membrane type was studied as a function of the amount of immobilized inhibitor and temperature. All active membranes have shown good inhibitory power. The most efficient membrane was that loaded with alpha(1)-antitrypsin, the less efficient that with BPTI.
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