Details
| Original language | English |
|---|---|
| Pages (from-to) | 1834-1839 |
| Number of pages | 6 |
| Journal | PROTEOMICS |
| Volume | 11 |
| Issue number | 9 |
| Publication status | Published - 25 Feb 2011 |
Abstract
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.
Keywords
- 2-D Blue native/SDS-PAGE, Blue native PAGE, Destabilization, Plant proteomics, Protein complex, SDS
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: PROTEOMICS, Vol. 11, No. 9, 25.02.2011, p. 1834-1839.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Low-SDS Blue native PAGE
AU - Klodmann, Jennifer
AU - Lewejohann, Dagmar
AU - Braun, Hans Peter
PY - 2011/2/25
Y1 - 2011/2/25
N2 - 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.
AB - 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.
KW - 2-D Blue native/SDS-PAGE
KW - Blue native PAGE
KW - Destabilization
KW - Plant proteomics
KW - Protein complex
KW - SDS
UR - http://www.scopus.com/inward/record.url?scp=79955009768&partnerID=8YFLogxK
U2 - 10.1002/pmic.201000638
DO - 10.1002/pmic.201000638
M3 - Article
C2 - 21413149
AN - SCOPUS:79955009768
VL - 11
SP - 1834
EP - 1839
JO - PROTEOMICS
JF - PROTEOMICS
SN - 1615-9853
IS - 9
ER -