Affinity purification of recombinant trypsinogen using immobilized ecotin
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Updated: Oct 30, 2026
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Identification of Protein Interacting Partners Using Tandem Affinity Purification
Published on: February 25, 2012
Z Lengyel1, G Pál, M Sahin-Tóth
1NAVIX, Inc., Camarillo, California 93012, USA.
Protein Expression and Purification
|March 31, 1998
Abstract:
Affinity purification of inactive precursors (zymogens) of serine proteases on protease inhibitor columns is not feasible, due to the weak interaction between canonical protease inhibitors and protease zymogens. In this study we demonstrate that immobilized ecotin, a unique protease inhibitor from Escherichia coli, provides a superior affinity matrix for the purification of trypsinogen and possibly other serine protease zymogens as well.
