An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant Blue

1972 ◽  
Vol 48 (2) ◽  
pp. 617-620 ◽  
Author(s):  
W. Diezel ◽  
G. Kopperschläger ◽  
E. Hofmann
Keyword(s):  
Brilliant Blue ◽  
Polyacrylamide Gels ◽  
Coomassie Brilliant Blue ◽  
New Type ◽  
Protein Staining ◽  
Coomassie Brilliant

scholarly journals Elution of proteins from polyacrylamide eels: a simple and economic procedure

1989 ◽  
Vol 31 (1) ◽  
pp. 44-47
Author(s):  
Vera Bongertz
Keyword(s):  
Gel Electrophoresis ◽  
Brilliant Blue ◽  
Polyacrylamide Gels ◽  
Coomassie Brilliant Blue ◽  
Coomassie Brilliant

A simplified methodology for the quantitative electroelution of proteins from polyacrylamide gels is described. After staining with Coomassie Brilliant Blue R 250, the identified bands are excised from the gel and the proteins eluted using a procedure developed for use in conventional tube gel electrophoresis equipment.

Interference of the carbohydrate moiety in Coomassie Brilliant Blue R-250 protein staining

1989 ◽  
Vol 10 (4) ◽  
pp. 271-273 ◽  
Author(s):  
Miquel Osset ◽  
Montserrat Piñol ◽  
Martin J. M. Fallon ◽  
Rafael De Llorens ◽  
Claudi M. Cuchillo
Keyword(s):  
Carbohydrate Moiety ◽  
Brilliant Blue ◽  
Coomassie Brilliant Blue ◽  
Protein Staining ◽  
Coomassie Brilliant

scholarly journals Combined quantitative cytophotometric method for staining indolyl and sulfhydryl groups and protein.

1983 ◽  
Vol 31 (7) ◽  
pp. 967-970 ◽  
Author(s):  
Y Nakae ◽  
M Shono ◽  
H Ishizuka
Keyword(s):  
Sulfhydryl Groups ◽  
Brilliant Blue ◽  
Quantitative Histochemistry ◽  
Coomassie Brilliant Blue ◽  
Protein Staining ◽  
Coomassie Brilliant

Sulfenylation with 2-nitrophenylsulfenyl chloride (NPS-Cl), which is specific for tryptophyl and cysteinyl residues in protein, was applied to quantitative histochemistry. By measurement of the absorbance values at 370 nm of sections stained with NPS-Cl, Beer-Lambert's law was found to hold for NPS staining. Treatment of NPS-stained sections with 2-mercaptoethanol (ME) (NPS-ME staining) resulted in sulfenylation of tryptophyl residues only. For determination of the amounts of tryptophyl and cysteinyl residues per unit of protein, protein staining with Coomassie Brilliant Blue (CB) was combined with NPS and NPS-ME staining. CB and NPS-CBB staining also followed Beer-Lambert's law. By measuring the absorbance values at 370 and 650 nm of doubly stained sections, the relative contents of tryptophyl and cysteinyl residues in various tissue proteins were calculated. This method will be useful for the investigation of changes in both protein amount and composition.

Coomassie-Brilliant Blue Staining of Polyacrylamide Gels

2012 ◽  
pp. 465-469 ◽  
Author(s):  
Claudia Arndt ◽  
Stefanie Koristka ◽  
Anja Feldmann ◽  
Holger Bartsch ◽  
Michael Bachmann
Keyword(s):  
Brilliant Blue ◽  
Blue Staining ◽  
Polyacrylamide Gels ◽  
Coomassie Brilliant Blue ◽  
Coomassie Brilliant Blue Staining ◽  
Coomassie Brilliant

scholarly journals Effect of pre-stain methanol washing on the sensitivity of CBBR-250 staining in SDS-polyacrylamide gels

2015 ◽  
Vol 2 (1) ◽  
Author(s):  
Rashid Saleem ◽  
Absar-ul Hasnain ◽  
Riaz Ahmad
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Staining Method ◽  
Muscle Protein ◽  
Brilliant Blue ◽  
Low Molecular Weight ◽  
Polyacrylamide Gels ◽  
Coomassie Brilliant Blue ◽  
Protein Research ◽  
Coomassie Brilliant

AbstractCoomassie Brilliant Blue R-250 (CBBR-250) is the most frequently used dye stain in protein research. However, relatively poor sensitivity and long application durations are the major limitations of this stain. In the present study, we have investigated the effect of pre-stain methanol washing on the sensitivity of the conventional CBB staining method. Concentrations of methanol ranging from 5 to 30% were prepared in 5% acetic acid. Pre-stain washing of SDS-gels using acetic acid (5%) and methanol were assessed at various timings and temperatures. Our results demonstrate that pre-stain washing by methanol greatly improves the sensitivity of the CBB stain and facilitates the visualization of low molecular weight components present in a complex muscle protein, actomyosin. The outcome of this study also revealed duration of pre-stain washing and temperature as other factors that determine the sensitivity of CBB staining method. Therefore, it is suggested that pre-stain washing with methanol may improve the sensitivity of CBB stain in SDS-PA gels.

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