A simple method for the extraction of Coomassie brilliant blue R from stained protein bands excised from polyacrylamide gels is described. Spectrophotometric measurement of the eluted dye forms the basis of a sensitive assay to quantitate proteins in gels in the range 0.5-10 micrograms. The method r
Extraction of proteins and peptides from Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gels
β Scribed by D.R. Gibson; R.W. Gracy
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 212 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A method is described for extracting proteins and peptides from stained sodium dodecyl sulfate-polyacrylamide gels. Coomassie blue and sodium dodecyl sulfate present in stained gel sections are removed to allow subsequent analysis of the peptides (e.g., amino acid analysis or tryptic digestion and fingerprinting). The method is simple, requires no radioisotopes or special equipment, and can be carried out with a minimum of handling of the sample. The process can be used for samples at the nanomole level with recoveries of 90%.
π SIMILAR VOLUMES
A simple method and apparatus are described for the efficient recovery of proteins from sodium dodecyl sulfate-polyacrylamide gel systems after electrophoretic resolution. This procedure provides for high yields of proteins which are free of sodium dodecyl sulfate and in certain cases, exhibit signi
## Quantitation of Submicrogram Amounts of Protein Using Coomassie Brilliant Blue R on Sodium Dodecyl Sulfate-Polyacrylamide Slab-Gels A sodium dodecyl sulfate (SDS)-polyacrylamide slab-gel system was used to study the use of Coomassie brilliant blue (CB) as a quantitative stain. Quantitation curv