Affinity purification of recombinant trypsinogen using immobilized ecotin

Zsolt Lengyel, Gábor Pál, Miklós Sahin-Tóth

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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.

Original languageEnglish
Pages (from-to)291-294
Number of pages4
JournalProtein Expression and Purification
Volume12
Issue number2
DOIs
Publication statusPublished - Mar 1998

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ASJC Scopus subject areas

  • Biotechnology

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