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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

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European Molecular Biology Laboratory (EMBL), Heidelberg, Germany
Cite this: Anal. Chem. 1996, 68, 5, 850–858
Publication Date (Web):March 1, 1996
https://doi.org/10.1021/ac950914h
Copyright © 1996 American Chemical Society

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    Abstract

    Proteins from silver-stained gels can be digested enzymatically and the resulting peptides analyzed and sequenced by mass spectrometry. Standard proteins yield the same peptide maps when extracted from Coomassie- and silver-stained gels, as judged by electrospray and MALDI mass spectrometry. The low nanogram range can be reached by the protocols described here, and the method is robust. A silver-stained one-dimensional gel of a fraction from yeast proteins was analyzed by nanoelectrospray tandem mass spectrometry. In the sequencing, more than 1000 amino acids were covered, resulting in no evidence of chemical modifications due to the silver staining procedure. Silver staining allows a substantial shortening of sample preparation time and may, therefore, be preferable over Coomassie staining. This work removes a major obstacle to the low-level sequence analysis of proteins separated on polyacrylamide gels.

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    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

     Abstract published in Advance ACS Abstracts, January 15, 1996.

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