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

Julian Borejdo; Carroll Flynn

doi:10.1016/0003-2697(84)90136-2

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

Julian Borejdo, Carroll Flynn

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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 language	English
Pages (from-to)	84-86
Number of pages	3
Journal	Analytical Biochemistry
Volume	140
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(84)90136-2
State	Published - Jul 1984

Keywords

Coomassie blue stain
gel staining
polyacrylamide gel electrophoresis

Access to Document

10.1016/0003-2697(84)90136-2

Cite this

@article{2a359721ffb841b9b88a6f482ee8e5b7,

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

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.",

keywords = "Coomassie blue stain, gel staining, polyacrylamide gel electrophoresis",

author = "Julian Borejdo and Carroll Flynn",

note = "Funding Information: J.B. is an Established Investigator of the American Heart Association. This research was supported by grants from US-Israel Binational Science Foundation, Muscular Dystrophy Association, and American Heart Association Grant-In-Aid 81-612.",

year = "1984",

month = jul,

doi = "10.1016/0003-2697(84)90136-2",

language = "English",

volume = "140",

pages = "84--86",

journal = "Analytical Biochemistry",

issn = "0003-2697",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Electrophoresis in the presence of Coomassie brilliant blue R-250 stains polyacrylamide gels during protein fractionation

AU - Borejdo, Julian

AU - Flynn, Carroll

N1 - Funding Information: J.B. is an Established Investigator of the American Heart Association. This research was supported by grants from US-Israel Binational Science Foundation, Muscular Dystrophy Association, and American Heart Association Grant-In-Aid 81-612.

PY - 1984/7

Y1 - 1984/7

N2 - 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.

AB - 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.

KW - Coomassie blue stain

KW - gel staining

KW - polyacrylamide gel electrophoresis

UR - http://www.scopus.com/inward/record.url?scp=0021459346&partnerID=8YFLogxK

U2 - 10.1016/0003-2697(84)90136-2

DO - 10.1016/0003-2697(84)90136-2

M3 - Article

C2 - 6207746

AN - SCOPUS:0021459346

SN - 0003-2697

VL - 140

SP - 84

EP - 86

JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 1

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this