Application of receptor-affinity chromatography to bioaffinity purification

Receptor-affinity chromatography based upon the receptor-ligand interactions has been utilized for the purification of recombinant human interleukin-2 (rIL-2) from microbial and mammalian sources. The receptor-affinity purification process of rIL-2 is used as a model system to demonstrate the utilit...

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Bibliographic Details
Published inJournal of chromatography Vol. 510; p. 59
Main Authors Weber, D V, Bailon, P
Format Journal Article
LanguageEnglish
Published Netherlands 27.06.1990
Subjects
Amino Acids - analysis
Animals
Biological Assay
Cells, Cultured
Chromatography, Affinity
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Immunosorbent Techniques
Interleukin-2 - isolation & purification
Ligands
Mice
Receptors, Drug - analysis
Recombinant Proteins - isolation & purification
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Summary:Receptor-affinity chromatography based upon the receptor-ligand interactions has been utilized for the purification of recombinant human interleukin-2 (rIL-2) from microbial and mammalian sources. The receptor-affinity purification process of rIL-2 is used as a model system to demonstrate the utility of this approach for the purification of recombinant proteins. The receptor-affinity purified biomolecule is shown to be biochemically and biologically more homogeneous than the immunoaffinity purified material.
DOI:10.1016/S0021-9673(01)93739-2