Low-SDS Blue native PAGE

authored by

Jennifer Klodmann, Dagmar Lewejohann, Hans Peter Braun

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.

Organisation(s)

Section Plant Molecular Biology and Plant Proteomics
Institute of Plant Genetics

Type

Article

Journal

PROTEOMICS

Volume

11

Pages

1834-1839

No. of pages

6

ISSN

1615-9853

Publication date

25.02.2011

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Biochemistry, Molecular Biology

Electronic version(s)

https://doi.org/10.1002/pmic.201000638 (Access: Unknown)