Electrophoresis in the presence of Coomassie brilliant blue R-250 stains polyacrylamide gels during protein fractionation
β Scribed by Julian Borejdo; Carroll Flynn
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 489 KB
- Volume
- 140
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A method of staining polyacrylamide gels in which the dye is electrophoresed together with the sample is proposed. The method cuts short and simplifies the conventional electrophoresis procedure by eliminating the separate poststaining step. In the gels run in the presence of sodium dodecyl sulfate, the method produces protein staining patterns which are quantitatively identical to the ones obtained by conventional staining procedure. Additional advantages of the method are easy control over the degree of staining and homogenous staining independent of the gel thickness and concentration of the dye.
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Destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels with sodium chloride solutions
A new staining procedure for proteins in polyacrylamide gels has been developed. This procedure, utilizing Coomassie brilliant blue G250, is rapid (as quick as 30 min) and simple to perform, requires little or no destaining, and has a sensitivity of a least 1 pg of protein per band. It can be used t
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