𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Electrophoresis in the presence of Coomassie brilliant blue R-250 stains polyacrylamide gels during protein fractionation

✍ Scribed by Julian Borejdo; Carroll Flynn


Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
489 KB
Volume
140
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ 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.


πŸ“œ SIMILAR VOLUMES


A new staining technique for proteins in
✍ Robert W. Blakesley; John A. Boezi πŸ“‚ Article πŸ“… 1977 πŸ› Elsevier Science 🌐 English βš– 180 KB

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

Quantitation of proteins by elution of C
✍ Eric H. Ball πŸ“‚ Article πŸ“… 1986 πŸ› Elsevier Science 🌐 English βš– 424 KB

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