Research Article
Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
Article first published online: 25 MAR 1999
DOI: 10.1002/(SICI)1522-2683(19990301)20:3<601::AID-ELPS601>3.0.CO;2-6
Copyright © 1999 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany
Additional Information
How to Cite
Gharahdaghi, F., Weinberg, C. R., Meagher, D. A., Imai, B. S. and Mische, S. M. (1999), Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity. ELECTROPHORESIS, 20: 601–605. doi: 10.1002/(SICI)1522-2683(19990301)20:3<601::AID-ELPS601>3.0.CO;2-6
Publication History
- Issue published online: 25 MAR 1999
- Article first published online: 25 MAR 1999
- Manuscript Received: 4 AUG 1998
- Abstract
- References
- Cited By
Keywords:
- Two-dimensional gel electrophoresis;
- Silver staining;
- Mass spectrometry;
- In-gel;
- Protein identification;
- Peptide mass mapping
Abstract
Mass spectrometry is a powerful technique for the identification of proteins at nanogram quantities. However, some degree of sample preparation prior to mass spectrometry is required, and silver-stained protein gel samples are most problematic. Here we report our strategy to obtain peptide mass profiles from silver-stained protein gel samples from one- or two-dimensional gels by destaining prior to enzymatic digestion. This study demonstrates that by using the destaining method, the sensitivity and quality of mass spectra is increased for matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric analysis, permitting more proteins to be identified by peptide mass database analysis.

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