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Updated: May 16, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

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

Boswellic acids and protease activities.

B Rall¹, H P Ammon, H Safayhi

¹Department of Pharmacology, Institute for Pharmazeutical Sciences, University of Tuebingen, Auf der Morgenstelle 8, D-72076 Tuebingen, Germany.

Phytomedicine : International Journal of Phytotherapy and Phytopharmacology

|December 1, 2012

Summary

This summary is machine-generated.

Acetyl-11-keto-β-boswellic acid (AKBA) was investigated for its effects on human leukocyte elastase (HLE), a key enzyme in inflammation. This study explored AKBA

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Area of Science:

Biochemistry
Enzymology
Pharmacology

Background:

Human leukocyte elastase (HLE) plays a significant role in inflammatory conditions.
Ursolic acid has demonstrated inhibitory effects on HLE.
Investigating novel inhibitors for HLE is crucial for managing inflammation.

Purpose of the Study:

To investigate the effects of acetyl-11-keto-β-boswellic acid (AKBA) on serine proteinases.
Specifically, to determine AKBA's impact on human leukocyte elastase (HLE).

Main Methods:

Enzyme inhibition assays were performed.
The study focused on serine proteinases, including HLE.
Acetyl-11-keto-β-boswellic acid (AKBA) was used as the test compound.

Main Results:

The abstract does not contain specific results.
Further investigation is needed to determine AKBA's inhibitory activity against HLE.

Conclusions:

The study initiated the investigation of AKBA's potential as an HLE inhibitor.
Understanding AKBA's interaction with serine proteinases could offer new therapeutic avenues for inflammatory diseases.