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Updated: Jan 22, 2026

Use of the Protease Fluorescent Detection Kit to Determine Protease Activity
Published on: August 4, 2009
Light scattering determination of the stoichiometry for protease-potato serine protease inhibitor complexes
Erika Billinger1, Shusheng Zuo1, Kristoffer Lundmark1
1Department of Chemistry - BMC Uppsala University, Box 576, SE-751 23, Uppsala, Sweden.
Abstract:
The interaction between pancreatic proteases and a serine protease inhibitor purified from potato tubers was investigated by chromatography-coupled light scattering measurements. The molar mass distribution in the chromatogram was compared to theoretical values calculated for the different possible combinations of complexes and free components by three different approaches, namely section analyses of the chromatograms, full mass average determination and mass distribution analysis. This revealed that the inhibitor was able to bind trypsin in a 2:1 complex, whereas the data for chymotrypsin clearly showed a limitation to 1:1 complex regardless of the molar ratio in the injected samples. The same experiment carried out with elastase and the potato inhibitor gave only weak indications of complex formation under the conditions used.
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