One-step purification of trypsin and α-chymotrypsin by affinity chromatography on Eupergit—aprotinin, a novel carrier for purification of serine proteases

Abstract

Aprotinin isolated from bovine lungs was covalently immobilized on Eupergit C. The highly selective affinity adsorbent was used to purify trypsin and α-chymotrypsin from pancreatic extract in a single step. Sodium dodecyl sulphate—polyacrylamide gel electrophoresis indicated that both enzymes were highly purified. The maximum binding capacity of Eupergit—aprotinin for bovine trypsin was calculated to be ca. 7.5 mg per gram of gel (wet resin).