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Blue-native PAGE in plants: a tool in analysis of protein-protein interactions

Intact protein complexes can be separated by apparent molecular mass using a standard polyacrylamide gel electrophoresis system combining mild detergents and the dye Coomassie Blue. Referring to the blue coloured gel and the gentle method of solubilization yielding native and enzymatically active pr...

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Detalles Bibliográficos
Autores principales: Eubel, Holger, Braun, Hans-Peter, Millar, A Harvey
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1308860/
https://www.ncbi.nlm.nih.gov/pubmed/16287510
http://dx.doi.org/10.1186/1746-4811-1-11
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author Eubel, Holger
Braun, Hans-Peter
Millar, A Harvey
author_facet Eubel, Holger
Braun, Hans-Peter
Millar, A Harvey
author_sort Eubel, Holger
collection PubMed
description Intact protein complexes can be separated by apparent molecular mass using a standard polyacrylamide gel electrophoresis system combining mild detergents and the dye Coomassie Blue. Referring to the blue coloured gel and the gentle method of solubilization yielding native and enzymatically active protein complexes, this technique has been named Blue-Native Polyacrylamide Gel-Electrophoresis (BN-PAGE). BN-PAGE has become the method of choice for the investigation of the respiratory protein complexes of the electron transfer chains of a range of organisms, including bacteria, yeasts, animals and plants. It allows the separation in two dimensions of extremely hydrophobic protein sets for analysis and also provides information on their native interactions. In this review we discuss the capabilities of BN-PAGE in proteomics and the wider investigation of protein:protein interactions with a focus on its use and potential in plant science.
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spelling pubmed-13088602005-12-08 Blue-native PAGE in plants: a tool in analysis of protein-protein interactions Eubel, Holger Braun, Hans-Peter Millar, A Harvey Plant Methods Review Intact protein complexes can be separated by apparent molecular mass using a standard polyacrylamide gel electrophoresis system combining mild detergents and the dye Coomassie Blue. Referring to the blue coloured gel and the gentle method of solubilization yielding native and enzymatically active protein complexes, this technique has been named Blue-Native Polyacrylamide Gel-Electrophoresis (BN-PAGE). BN-PAGE has become the method of choice for the investigation of the respiratory protein complexes of the electron transfer chains of a range of organisms, including bacteria, yeasts, animals and plants. It allows the separation in two dimensions of extremely hydrophobic protein sets for analysis and also provides information on their native interactions. In this review we discuss the capabilities of BN-PAGE in proteomics and the wider investigation of protein:protein interactions with a focus on its use and potential in plant science. BioMed Central 2005-11-16 /pmc/articles/PMC1308860/ /pubmed/16287510 http://dx.doi.org/10.1186/1746-4811-1-11 Text en Copyright © 2005 Eubel et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Eubel, Holger
Braun, Hans-Peter
Millar, A Harvey
Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title_full Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title_fullStr Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title_full_unstemmed Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title_short Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
title_sort blue-native page in plants: a tool in analysis of protein-protein interactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1308860/
https://www.ncbi.nlm.nih.gov/pubmed/16287510
http://dx.doi.org/10.1186/1746-4811-1-11
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