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CiteWeb id: 19960000039

CiteWeb score: 8374

DOI: 10.1021/ac950914h

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.

The publication "Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels" is placed in the Top 10000 of the best publications in CiteWeb. Also in the category Chemistry it is included to the Top 100. Additionally, the publicaiton "Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels" is placed in the Top 100 among other scientific works published in 1996.
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