Journal
PROTEOMICS
Volume 11, Issue 9, Pages 1834-1839Publisher
WILEY
DOI: 10.1002/pmic.201000638
Keywords
2-D Blue native/SDS-PAGE; Blue native PAGE; Destabilization; Plant proteomics; Protein complex; SDS
Funding
- Deutsche Forschungsgemeinschaft (DFG) [Br1829/8-1, Br1829/10-1]
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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.
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