Quantitative investigation of the affinity properties of different recombinant forms of protein G by means of high-performance monolithic chromatography
| Autor: | V. G. Palagnuk, Gupalova Tv, Artem A. Totolian, O.V Lojkina, Tatiana B. Tennikova |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Monolithic HPLC column
Chromatography biology Chemistry G protein Organic Chemistry Serum albumin Enzyme-Linked Immunosorbent Assay Nerve Tissue Proteins General Medicine Biochemistry Immunoglobulin G Chromatography Affinity Recombinant Proteins Analytical Chemistry Dissociation constant chemistry.chemical_compound Affinity chromatography biology.protein Electrophoresis Polyacrylamide Gel Protein G Adsorption Bifunctional Chromatography High Pressure Liquid |
| Zdroj: | Journal of chromatography. A. 949(1-2) |
| ISSN: | 0021-9673 |
| Popis: | The recombinantly produced different forms of protein G, namely monofunctional immunoglobulin G (IgG) binding, monofunctional serum albumin (SA) binding and bifunctional IgG/SA binding proteins G, are compared with respect to their specific affinities to blood IgG and SA. The affinity mode of the recently developed high-performance monolithic disk chromatography has been used for fast quantitative investigations. Using single affinity disks as well as two discs stacked into one separation unit, one order of magnitude in adsorption capacities for IgG and SA were found both for monofunctional and bifunctional protein G forms used as specific affinity ligands. However, despite the adsorption difference observed, the measured dissociation constants of the affinity complexes seemed to be very close. The analytical procedure developed can be realized within a couple of minutes. Up-scaling of the developed technology was carried out using another type of monolithic materials, i.e. CIM affinity tubes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect