Fluidized-bed receptor-affinity chromatography
| Autor: | Pascal Bailon, Cheryl Spence, Carol Ann Schaffer, Stephen B. Kessler |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Sorbent
Virulence Factors medicine.drug_class Bacterial Toxins Clinical Biochemistry Exotoxins Monoclonal antibody Biochemistry Chromatography Affinity Cell Line Analytical Chemistry law.invention Affinity chromatography Immunotoxin law Drug Discovery medicine Humans Molecular Biology ADP Ribose Transferases Pharmacology Chromatography Chemistry Immunotoxins Antibodies Monoclonal Receptors Interleukin-2 General Medicine Recombinant Proteins Fluidized bed Recombinant DNA Interleukin-2 Target protein Protein ligand |
| Zdroj: | Biomedical Chromatography. 8:236-241 |
| ISSN: | 1099-0801 0269-3879 |
| DOI: | 10.1002/bmc.1130080508 |
| Popis: | A multipurpose fluidized-bed receptor-affinity purification system based upon the biological recognition between an immobilized receptor and its soluble protein ligands is described. The fluidized affinity sorbent consists of a soluble form of interleukin-2 receptor chemically bonded to an aldehyde derivative of controlled pore glass beads, which have a pore diameter of 1000 A and a particle density of 1.2-1.3 g/mL. The fluidized-bed separation device used in this study consists of a specially designed column fitted at the inlet end with a perforated distributor plate covered with a screen and the top outlet with an adjustable piston. The fluidized-bed consisting of a loose gel matrix permits the unimpeded passage of cell debris and particulate matter, while the target protein is captured by the affinity beads. Purification of the humanized-anti-Tac monoclonal antibody is used as a model system to determine the operational parameters. Also, fluidized-bed receptor-affinity chromatography has been successfully employed in the purification of recombinant interleukin-2 and single chain anti-Tac(Fv)-Pseudomonas exotoxin immunotoxin from unclarified inclusion body extracts. Overall, fluidized-bed receptor-affinity chromatography is found to be a productive affinity method suitable for the purification of recombinant human interleukin-2 and related molecules. |
| Databáze: | OpenAIRE |
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