Low-SDS Blue native PAGE

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OriginalspracheEnglisch
Seiten (von - bis)1834-1839
Seitenumfang6
FachzeitschriftPROTEOMICS
Jahrgang11
Ausgabenummer9
PublikationsstatusVeröffentlicht - 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.

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Low-SDS Blue native PAGE. / Klodmann, Jennifer; Lewejohann, Dagmar; Braun, Hans Peter.
in: PROTEOMICS, Jahrgang 11, Nr. 9, 25.02.2011, S. 1834-1839.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Klodmann J, Lewejohann D, Braun HP. Low-SDS Blue native PAGE. PROTEOMICS. 2011 Feb 25;11(9):1834-1839. doi: 10.1002/pmic.201000638
Klodmann, Jennifer ; Lewejohann, Dagmar ; Braun, Hans Peter. / Low-SDS Blue native PAGE. in: PROTEOMICS. 2011 ; Jahrgang 11, Nr. 9. S. 1834-1839.
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AU - Klodmann, Jennifer

AU - Lewejohann, Dagmar

AU - Braun, Hans Peter

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KW - Destabilization

KW - Plant proteomics

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