Affinity purification of recombinant trypsinogen using immobilized ecotin.
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.
Lengyel
Z
Z
NAVIX, Inc., Camarillo, California 93012, USA.
Pál
G
G
Sahin-Tóth
M
M
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D051381:Rats; D014361:Trypsin Inhibitors / Q000737:chemistry*; D014362:Trypsinogen / Q000302:isolation & purification*
D001426:Bacterial Proteins; C039076:Eco protein, E coli; D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D014361:Trypsin Inhibitors; D014362:Trypsinogen