Protein Staining Influences the Quality of Mass Spectra Obtained by Peptide Mass Fingerprinting after Separation on 2-D Gels. A Comparison of Staining with Coomassie Brilliant Blue and Sypro Ruby

2005 ◽  
Vol 4 (1) ◽  
pp. 175-179 ◽  
Author(s):  
Boel Lanne ◽  
Oleg Panfilov
Keyword(s):  
Mass Spectra ◽  
Peptide Mass Fingerprinting ◽  
Brilliant Blue ◽  
Coomassie Brilliant Blue ◽  
Peptide Mass ◽  
Protein Staining ◽  
Coomassie Brilliant

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.

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