In:
PROTEOMICS, Wiley, Vol. 11, No. 9 ( 2011-05), p. 1834-1839
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.
Type of Medium:
Online Resource
ISSN:
1615-9853
,
1615-9861
DOI:
10.1002/pmic.201000638
Language:
English
Publisher:
Wiley
Publication Date:
2011
detail.hit.zdb_id:
2037674-1
SSG:
12
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