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

Julian Borejdo, Carroll Flynn

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)84-86
Number of pages3
JournalAnalytical Biochemistry
Volume140
Issue number1
DOIs
StatePublished - 1 Jan 1984

Fingerprint

Fractionation
Electrophoresis
Coloring Agents
Gels
Staining and Labeling
Sodium Dodecyl Sulfate
Proteins
polyacrylamide gels
Coomassie brilliant blue R

Keywords

  • Coomassie blue stain
  • gel staining
  • polyacrylamide gel electrophoresis

Cite this

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Electrophoresis in the presence of Coomassie brilliant blue R-250 stains polyacrylamide gels during protein fractionation. / Borejdo, Julian; Flynn, Carroll.

In: Analytical Biochemistry, Vol. 140, No. 1, 01.01.1984, p. 84-86.

Research output: Contribution to journalArticle

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AU - Flynn, Carroll

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