Comparison of Coomassie Brilliant Blue protein dye-binding assays for determination of urinary protein concentration.

Abstract We investigated the influence of assay protocol upon results of Coomassie Brilliant Blue protein dye-binding assays for urinary protein. Sensitivity and working range for, and linearity of response (including dilution dependence) of, three standard assays and four micro assays to bovine albumin, gamma-globulin, and urine are compared. The Read and Northcote standard assay (Anal Biochem 1981; 116:53-64) appears to be the method of choice.

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Interference in the Coomassie Brilliant Blue and Pyrogallol Red protein dye-binding assays is increased by the addition of sodium dodecyl sulfate to the dye reagents

Analytical Biochemistry ◽

10.1016/j.ab.2004.04.029 ◽

2004 ◽

Vol 331 (2) ◽

pp. 255-259 ◽

Cited By ~ 10

Author(s):

Thomas Marshall ◽

Katherine M Williams

Keyword(s):

Sodium Dodecyl Sulfate ◽

Sodium Dodecyl ◽

Brilliant Blue ◽

Binding Assays ◽

Coomassie Brilliant Blue ◽

Pyrogallol Red ◽

Dodecyl Sulfate ◽

Dye Binding ◽

Coomassie Brilliant

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Coomassie brilliant blue G-250 dye-binding technique for determination of autolytic protein breakdown in Euglena gracilis and comparison to other methods of autolysis measurement

Analytical Biochemistry ◽

10.1016/0003-2697(86)90088-6 ◽

1986 ◽

Vol 153 (2) ◽

pp. 242-250 ◽

Cited By ~ 17

Author(s):

Rainald Krauspe ◽

Angelika Scheer

Keyword(s):

Euglena Gracilis ◽

Brilliant Blue ◽

Protein Breakdown ◽

Brilliant Blue G ◽

Coomassie Brilliant Blue ◽

Dye Binding ◽

Coomassie Brilliant

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Total protein determined in human breast milk by use of coomassie brilliant blue and centrifugal analysis.

Clinical Chemistry ◽

10.1093/clinchem/35.10.2127 ◽

1989 ◽

Vol 35 (10) ◽

pp. 2127-2129 ◽

Cited By ~ 14

Author(s):

Y Bergqvist ◽

L Karlsson ◽

L Fohlin

Keyword(s):

Breast Milk ◽

Total Protein ◽

Brilliant Blue ◽

Human Breast Milk ◽

Human Breast ◽

Simple Method ◽

Coomassie Brilliant Blue ◽

Kjeldahl Method ◽

Coomassie Brilliant

Abstract This simple method of centrifugal analysis for total protein in human breast milk is based on the change in the wavelength of the absorbance maximum of Coomassie Brilliant Blue G-250 when the dye is bound to protein. Within-run and between-day CVs were 3.8% and 4.8%, respectively. Compared with a micro-Kjeldahl method for determination of total nitrogen, the coefficient of correlation was 0.99.

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Aggregation of a Dye on a Surfactant: Interaction of Coomassie Brilliant Blue G250 with Cetyltrimethylammonium Bromide and Determination of the Cationic Surfactant in Water

Instrumentation Science & Technology ◽

10.1081/ci-120030539 ◽

2004 ◽

Vol 32 (3) ◽

pp. 271-280 ◽

Cited By ~ 7

Author(s):

Hong‐Wen Gao ◽

Li‐Xin Zheng ◽

Hou‐Dong Mei

Keyword(s):

Cationic Surfactant ◽

Cetyltrimethylammonium Bromide ◽

Brilliant Blue ◽

Coomassie Brilliant Blue ◽

Coomassie Brilliant

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Automatic assay of urinary protein using Coomassie Brilliant Blue G-250

Analytical Biochemistry ◽

10.1016/0003-2697(81)90066-x ◽

1981 ◽

Vol 113 (1) ◽

pp. 197-201 ◽

Cited By ~ 11

Author(s):

Kiyoko Sano ◽

Kiyoko Kanamori ◽

Akihiko Shiba ◽

Makoto Nakao

Keyword(s):

Urinary Protein ◽

Brilliant Blue ◽

Brilliant Blue G ◽

Coomassie Brilliant Blue ◽

Coomassie Brilliant

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Coomassie Brilliant Blue-binding: a simple and effective method for the determination of water-insoluble protein surface hydrophobicity

Analytical Methods ◽

10.1039/c5ay02630j ◽

2016 ◽

Vol 8 (4) ◽

pp. 790-795 ◽

Cited By ~ 6

Author(s):

Yungang Cao ◽

Jing Zhao ◽

Youling L. Xiong

Keyword(s):

Surface Hydrophobicity ◽

Fluorescence Method ◽

Brilliant Blue ◽

Insoluble Protein ◽

Protein Surface ◽

Coomassie Brilliant Blue ◽

Protein Surface Hydrophobicity ◽

Coomassie Brilliant

A novel Coomassie Brilliant Blue-binding method, which correlated well with the widely accepted ANS fluorescence method (R = 0.95), was developed to determine the surface hydrophobicity of water-insoluble proteins.

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

Journal of Histochemistry & Cytochemistry ◽

10.1177/31.7.6854009 ◽

1983 ◽

Vol 31 (7) ◽

pp. 967-970 ◽

Cited By ~ 4

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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