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Anal Biochem. 2011 May 15;412(2):217-23. doi: 10.1016/j.ab.2011.01.038. Epub 2011 Feb 1.

High-resolution Native-PAGE for membrane proteins capable of fluorescence detection and hydrodynamic state evaluation.

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  • 1Molecular Signaling Research Team, Structural Physiology Research Group, RIKEN SPring-8 Center, Kouto, Sayo, Hyogo 679-5148, Japan.


An improved native polyacrylamide gel electrophoresis (PAGE) method capable of evaluating the hydrodynamic states of membrane proteins and allowing in-gel fluorescence detection was established. In this method, bis(alkyl) sulfosuccinate is used to provide negative charges for detergent-solubilized membrane proteins to facilitate proper electrophoretic migration without disturbing their native hydrodynamic states. The method achieved high-resolution electrophoretic separation, in good agreement with the elution profiles obtained by size exclusion chromatography. The applicability of in-gel fluorescence detection for tagged green fluorescent protein (GFP) facilitates the analysis of samples without any purification. This method might serve as a general analytical technique for assessing the folding, oligomerization, and protein complex formation of membrane proteins.

Copyright © 2011 Elsevier Inc. All rights reserved.

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