Isolation of Trypsin from Bovine Pancreas Using Immobilized Benzamidine and Peptide CTPR Ligands in Expanded Beds

Peptide CTPR and p-amino benzamidine (PAB) immobilized on Streamline™ were utilized as the chromatographic matrices for trypsin purification from bovine pancreas. By using a clarified pancreas extract, maximum capacity for CTPR-Streamline was 47.4 mg/mL and for PAB-Streamline 78.9 mg/mL while Kd val...

Full description

Saved in:
Bibliographic Details
Published in:Separation science and technology 2005-12, Vol.40 (16), p.3277-3287
Main Authors: Iannucci, Nancy B., Albanesi, Guillermo J., Marani, Mariela M., Fernández Lahore, Hector M., Cascone, Osvaldo, Camperi, Silvia A.
Format: Article
Language:English
Subjects:
Affinity
expanded bed
p-aminobenzamidine
peptide
trypsin
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Peptide CTPR and p-amino benzamidine (PAB) immobilized on Streamline™ were utilized as the chromatographic matrices for trypsin purification from bovine pancreas. By using a clarified pancreas 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 in the expanded-bed adsorption mode, 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.
ISSN:0149-6395
1520-5754
DOI:10.1080/01496390500423631