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 f
Quantitation of proteins by elution of Coomassie brilliant blue R from stained bands after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
โ Scribed by Eric H. Ball
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 424 KB
- Volume
- 155
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
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 requires no unusual equipment and is suitable for measurement of multiple samples. The polypeptide is not extracted and remains available for further analysis. The technique has been applied to three proteins and gels of various acrylamide percentages.
๐ SIMILAR VOLUMES
## 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