Low-SDS Blue native PAGE
| Autor: | Jennifer Klodmann, Hans-Peter Braun, Dagmar Lewejohann |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Proteomics
Chromatography Electron Transport Complex I biology Proteome Native gel electrophoresis Chemistry Arabidopsis Proteins Arabidopsis Reproducibility of Results Model system Native page biology.organism_classification Biochemistry Mitochondrial Proteins Electrophoresis Biophysics Electrophoresis Gel Two-Dimensional Molecular Biology Polyacrylamide gel electrophoresis |
| Zdroj: | Proteomics. 11(9) |
| ISSN: | 1615-9861 |
| Popis: | SDS normally is strictly avoided during Blue native (BN) PAGE because it leads to disassembly of protein complexes and unfolding of proteins. Here, we report a modified BN-PAGE procedure, which is based on low-SDS treatment of biological samples prior to native gel electrophoresis. Using mitochondrial OXPHOS complexes from Arabidopsis as a model system, low SDS concentrations are shown to partially dissect protein complexes in a very defined and reproducible way. If combined with 2-D BN/SDS-PAGE, generated subcomplexes and their subunits can be systematically investigated, allowing insights into the internal architecture of protein complexes. Furthermore, a 3-D BN/low-SDS BN/SDS-PAGE system is introduced to facilitate structural analysis of individual protein complexes without their previous purification. |
| Databáze: | OpenAIRE |
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