NDLI: Analysis of Electroblotted Proteins by Mass Spectrometry: Protein Identification after Western Blotting

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Analysis of Electroblotted Proteins by Mass Spectrometry: Protein Identification after Western Blotting

Content Provider	PubMed Central
Author	Luque-garcia, Jose L. Zhou, Ge Spellman, Daniel S. Sun, Tung-tien Neubert, Thomas A.
Abstract	We describe a new approach for the identification and characterization by mass spectrometry of proteins that have been electroblotted onto nitrocellulose. Using this method (Blotting And Removal of Nitrocellulose, or BARN), proteins can be analyzed either as intact proteins for molecular weight determination or as peptides generated by on-membrane proteolysis. Acetone is used to dissolve the nitrocellulose and to precipitate the adsorbed proteins/peptides, thus removing the nitrocellulose which can interfere with mass spectrometry analysis. This method offers improved protein coverage, especially for membrane proteins such as uroplakins, since the extraction step after in-gel digestion is avoided. Moreover, removal of nitrocellulose from the sample solution allows sample analysis by both MALDI- and (LC) ESI-based mass spectrometers. Finally, we demonstrate the utility of BARN for the direct identification of soluble and membrane proteins after Western blotting, obtaining comparable or better results than with in-gel digestion.
Related Links	http://dx.doi.org/10.1074/mcp.m700415-mcp200
Ending Page	314
Page Count	7
Starting Page	308
File Format	PDF
ISSN	15359476
e-ISSN	15359484
Journal	Molecular & cellular proteomics : MCP
Issue Number	2
Volume Number	7
Language	English
Publisher Date	2007-10-01
Access Restriction	Open
Subject Keyword	Analytical Chemistry Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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