Affordable Access

deepdyve-link
Publisher Website

Light scattering determination of the stoichiometry for protease-potato serine protease inhibitor complexes.

Authors
  • Billinger, Erika1
  • Zuo, Shusheng1
  • Lundmark, Kristoffer1
  • Johansson, Gunnar2
  • 1 Department of Chemistry - BMC Uppsala University, Box 576, SE-751 23, Uppsala, Sweden. , (Sweden)
  • 2 Department of Chemistry - BMC Uppsala University, Box 576, SE-751 23, Uppsala, Sweden. Electronic address: [email protected] , (Sweden)
Type
Published Article
Journal
Analytical Biochemistry
Publisher
Elsevier
Publication Date
Jul 02, 2019
Volume
582
Pages
113357–113357
Identifiers
DOI: 10.1016/j.ab.2019.113357
PMID: 31276650
Source
Medline
Keywords
Language
English
License
Unknown

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. Copyright © 2019 Elsevier Inc. All rights reserved.

Report this publication

Statistics

Seen <100 times