One-step purification of trypsin and alpha-chymotrypsin by affinity chromatography on Eupergit-aprotinin, a novel carrier for purification of serine proteases.
Aprotinin isolated from bovine lungs was covalently immobilized on Eupergit C. The highly selective affinity adsorbent was used to purify trypsin and alpha-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).
Schmitt
S
S
R-Biopharm GmbH, Darmstadt, F.R.G.
Goetschel
J D
JD
Römmelt
E M
EM
Adler
C
C
D007611:Aprotinin; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D014357:Trypsin / Q000302:isolation & purification*
C065842:Eupergit-aprotinin; D007611:Aprotinin; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin