CAMPERI Silvia Andrea
Isolation of Trypsin from Bovine Pancreas Using Immobilized Benzamidine and Peptide CTPR Ligands in Expanded Beds
N. B. IANNUCCI; G. J. ALBANESI; M. M. MARANI; H. M. FERNÁNDEZ LAHORE; O. CASCONE; S. A. CAMPERI
SEPARATION SCIENCE AND TECHNOLOGY
Taylor & Francis Group
Año: 2005 vol. 40 p. 3277 - 3277
Peptide CTPR and p-amino benzamidine (PAB) immobilised on StreamlineTM were utilised as the chromatographic matrices for trypsin purification from bovine pancreas. By using a clarified extract, maximum capacity for CTPR-Streamline was 47.4 mg/ml and for PAB-Streamline 78.9 mg/ml while Kd values were 0.39 and 0.38 respectively. Dynamic capacity was 23.0 and 46.0 mg/ml for CTPR- and PAB-Streamline respectively. When the purification process was applied to unclarified pancreas extract, 80 % trypsin recovery with a purification factor of 18.7 was achieved. Cationic and anionic trypsin obtained from the affinity column were separated by ion-exchange chromatography.