Recombinant proteins L and LG: efficient tools for purification of murine immunoglobulin G fragments
| Autor: | L. Tarditi, M. Mariani, R. Vola, A. Lombardi, L. Björck |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
medicine.drug_class
Monoclonal antibody Chromatography Affinity Immunoglobulin G law.invention Mice Bacterial Proteins Affinity chromatography law medicine Animals Immunoglobulin Fragments Chromatography biology Peptostreptococcus Chemistry Antibodies Monoclonal Radioimmunoassay General Chemistry Molecular biology Monoclonal immunoglobulin G Recombinant Proteins Protein L biology.protein Recombinant DNA Spectrophotometry Ultraviolet Antibody |
| Zdroj: | Journal of Chromatography B: Biomedical Sciences and Applications. 668:209-218 |
| ISSN: | 0378-4347 |
| DOI: | 10.1016/0378-4347(95)00091-v |
| Popis: | In order to improve antibody purification methods, recombinant proteins L and LG were tested in the purification of murine monoclonal immunoglobulin G (IgG) and its fragments. After affinity constant evaluation in different buffer systems, high-performance affinity chromatographic columns were prepared by coupling the proteins to Affi-prep 10 resin and tested with eight different murine monoclonal antibodies and their fragments of different isotypes. Affinity chromatographic experiments confirmed radioimmunoassay results showing that protein L bound 75% of the tested antibody fragments whereas protein LG had affinity for all the tested fragments. These results demonstrate that protein LG is the most powerful Ig-binding tool so far described. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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