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Scale-up of affinity chromatography for purification of enzymes and other proteins
- Source :
-
Enzyme & Microbial Technology . Sep2003, Vol. 33 Issue 4, p430. 8p. - Publication Year :
- 2003
-
Abstract
- Affinity chromatography uses biospecific binding usually between an antibody and an antigen, an enzyme and a substrate or other pairs of key-lock type of matching molecules. Due to its high selectivity, it is able to purify proteins and other macromolecules from very dilute solutions. In this work, a general rate model for affinity chromatography was used for scale-up studies. Parameters for the model were estimated from existing correlations, or from experimental results obtained on a small column with the same packing material. As an example, Affi-Gel with 4.5 μmol cm−3 Cibacron Blue F-3GA as immobilized ligands covalently attached to cross-linked 6% agarose was used for column packing. Cibacron Blue F-3GA was also used as a soluble ligand in the elution stage. Two separate cases were studied. One involved a bovine serum albumin solution, and the other hen egg white lysozyme solution. Satisfactory scale-up predictions were obtained for a 98.2 ml column and a 501 ml column based on a few experimental data obtained on a 7.85 ml small column. [Copyright &y& Elsevier]
- Subjects :
- *AFFINITY chromatography
*IMMUNE complexes
*MACROMOLECULES
*SERUM albumin
Subjects
Details
- Language :
- English
- ISSN :
- 01410229
- Volume :
- 33
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Enzyme & Microbial Technology
- Publication Type :
- Academic Journal
- Accession number :
- 10636343
- Full Text :
- https://doi.org/10.1016/S0141-0229(03)00141-8