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Protein Expr Purif. 1998 Mar;12(2):291-4.

Affinity purification of recombinant trypsinogen using immobilized ecotin.

Author information

1
NAVIX, Inc., Camarillo, California 93012, USA.

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.

PMID:
9518472
DOI:
10.1006/prep.1997.0837
[Indexed for MEDLINE]

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